Questions related to Imaging
I'm facing a real problem when trying to export data results from imageJ (fiji) to excel to process it later.
The problem is that I have to change manually the dots (.) , commas (,) even when changing the properties in excel (from , to .) in order not count the numbers as thousands, (let's say I have 1,302 = one point three zero two) it count it as (1302 = one thousand three hundred and two) when I transfer to excel...
Lately I found a nice plugin (Localized copy...) that can change the numbers format locally in imageJ so it can be used easily by excel.
Unfortunately, this plugin has some bugs because it can only copy one line of the huge data that I have and only for one time (so I have to close and reopen the image again).
is there anyone that has faced this problem? Can anyone suggest me please another solutions??
Thanks in advance
Problem finally solved... I got the new version of 'Localized copy' plugin from the owner Mr Wolfgang Gross (not sure if I have the permission to upload it here).
I want to calculate T1 relaxation time of Magnevist from phantom image. I have phantom images corresponding to the different dilution of magnevist and water at different repetition time (TR). I have calculated voxel intensity (from MIPAV) of these phantom images and that is the only data that I have. how can I calculate T1 relaxation time from this data?
I'm imaging hydroxyapatite particles with regular brightfield microscopy. I'm however struggling to find an explanation why the color of these particles differs depending on size. The smaller particles (~2 um) are often yellow or white, while the bigger particles (~50u um) are black. Could someone explain how the imaging techniques justifies these changes in colour?
Brain Tumor Imaging Protocol will reduce variability and increase accuracy in determining progression and response of investigational therapies.
In the pictures below, with the FFT and DFT methods and the PCA phase recovery, which is common in optical microscopes, I obtained the magnetic resonance imaging (MRI) phase of the human brain tumor and the phase obtained.
Can the process be performed on MRI without prescribing Jumpstarting Drugs (JBTDDC)?
I am trying to image live primary cells with Annexin V as a detector of PS exposure. I've currently been imaging in RPMI with 5% FBS, but I have realised that the calcium level of this may be too low for realiable Annexin V binding, as RPMI has a low calcium level of 0.42mM. Annexin V binding seems to require 1-3mM.
Other labs have successfully used complete DMEM with 10% FBS, would it be appropriate to use this for imaging even if I usually culture the cells in RMPI 5% FBS? Or should I try adding calcium (via calcium chloride) to my RPMI 5% media?
Thanks for any help.
Hi! I am trying to prepare hydroxyapatite scaffold samples for SEM imaging of cell growth. I have the Karnovsky's fixative kit but the procedure provided in the tech sheet (attached) is not sufficient for my applications. First, does anyone have a standard protocol for this SEM fixation using Karnovsky's fixative kit? Second, do I need to do the post-fix using OsO4 or is there an alternative method to the post-fix mentioned in the tech sheet? Can I do the fixation procedure without it, followed by the graded ethanol dehydration or will it have a negative impact on my sample preparation?
I would really appreciate any help answering this question. Thanks!
I want to measure the drug accumulation in semi-quantitative and quantitative method in the lung cell cultures (A549 cells). In this regard, my target is to measure it in a label free method as adding fluorophore to a drug changes its pharmacology.
I am facing some issue regarding the sample preparation of FFPE tissue for the MALDI mass spectrometry Imaging.
As many protocols suggest I tried pulse boiling the slides in a citric acid solution in a microwave for 10 min. Unfortunately because of heat and air bubbles the tissue sections came off during this step.
I already tried some less harsh methods, by heating in the same solution on a heating block (no bubbles, lower temperature) but judging the spectra of these samples the antigen retrieval did not seem to work properly here.
I am happy to receive some tipps and hear from your experience.
According to Lovett-Barron, 2021, zebrafish is the only vertebrate in which whole-brain imaging at once has been done. Since then have there been any other vertebrates in which the said strategy is implemented?
Are there any tips for obtaining clear images (20x) of cell files in each zone of Arabidopsis roots?
I normally fix them first in 96% ethanol and mount them in chloral hydrate. However, due to the ethanol, the roots are wrinkled, starting at the elongation zone (the meristem is okay).
Reducing the timing of ethanol clearing does not alter this effect, nor does using a lower percentage of ethanol, as observed in my samples with GUS-staining which are conserved at 70%.
I could try increasing the percentage, but this will be time consuming to apply to each sample.
Does anyone have any other ideas?
In order to perform time-lapse imaging of collagen-embedded spheroids, collagen drops (about 20 µl per drop) containing spheroids are spotted onto an Ibidi glass bottom 8 well slide (1 collagen drop/well) and allowed to polymerize during 2 hours. After collagen polymerization, culture medium (250-300 µl) is added to each well and time-lapse imaging of the 8 wells is performed overnight.
However, we frequently encounter a problem of gel detachment from the glass bottom slide during the overnight image acquisition step, which precludes a correct imaging of the spheroids embedded into these gels.
Has anyone already faced a similar situation and how can we improve the adhesion of the collagen drops to the glass bottom slides?
Thank you in advance for your precious collaboration.
We are fixing our tissue with 10% buffered formaldehyde. Before imaging, in order to recover the native structure of the biomolecules, I am treating the deparaffinized tissues with periodic acid in dark to recover the native structure of molecules within the tissue. I am looking for articles that specifically address this problem. A lot of immunohistochemistry is done, which ideally should not be possible if native structure biomolecules/antigen is not preserved. So, I am looking for articles discussing these issues. If anyone can share some links it will be a great help.
I have already used COMSOL, FDTD, and CST software, But they do not offer to map the near and far field distribution at the same simulation area around the particle. Is there any way to simulate near and far field distribution with same simulation area???
basically, i want to differentiate in the spatial distribution in the far field and near field.
I am working in research center that will provide verity of services for researchers and scientists who has interest to do research on lab animals. One of the services is to provide advance imaging platform, to do small animal imaging by using different techniques.
My question for who had an experience with the below two machines, please provide me with your suggestions and or recommendations which one of them is the best and are you willing to recommend one of them to your institution?
Thank you for your help
1-In-Vivo Xtreme II from Bruker https://www.bruker.com/products/preclinical-imaging/opticalx-ray-imaging/in-vivo-xtreme-ii/overview.html
2- IVIS Spectrum from PerkinElmer http://www.perkinelmer.com/product/ivis-instrument-spectrum-120v-andor-c-124262
I am looking for a commercially available fluorescent turn-ON (!) probe for imaging that detects ferric (3+) iron. I am aware of several publications that describe the synthesis and validate the probe. However, I can't find a commercial product that I need since I don't have the expertise for the synthesis.
The term "phase" is always a confusing thing for me. When we recoding images, we say that we have recorded the amplitude and phase. Amplitude I am able to relate/ physically understand by connecting with intensity. As, intensity increases, the amplitude will also increase. But the phase term is still I am not able to digest. I am not able physically understand the phase term, like understand the amplitude term. Can anyone explain this?
I have studied the mathematics of Phase. But I am not able to physically relate it.
I am trying to set up a TMRM-based assessment of mitochondrial membrane potential in fibroblast cells.
The aim of the study is to measure TMRM fluorescence at a high scale level (on 96 wells plates), in order to set up a High Throughput screening of molecules. The problem is that between the first and the last well, the signal is fading away abnormally fast. Although the plate is kept in dark at 37°C during the measure (around 30 min measure).
I have tried other probes less sensitives such as Mitotracker Orange, also dependent on mitochondrial potential and i don't see such fading (unless when I add FCCP of course), which indicates that it is not related to loss of membrane potential.
I have tried several incubation with TMRM, or after TMRM treatment, several concentrations (from 5 to 500 nM), and several buffers (PBS, cell culture medium). And of course I have tried to buy a new lot of TMRM
The result is always the same and I don't find anything explaining such a thing is the literature. The only thing described is that TMRM fluorescence can be auto-quenched when using high concentrations (more than 50 nM).
I really don't see what could be wrong... Has any of you already experienced something similar with TMRM? Would you have any idea how to fix it?
Thank you in advance for your help!!
I am currently trying to stain for PI3KBeta in MDA-MB-231 cells. My current issue is that 1) beta stains all over the cell and 2) there is an increase in signal at the edge of the cell and this increase in signal co-localizes with cellular ruffles (imaged in phase). My goal is to look at PI3Kbeta's recruitment to the plasma membrane in response to growth factor stimulation; however, an increase in staining at the edge of the cell that may be due to ruffling makes it very difficult to study this. Does anyone have any tips/experience/references that can help me analyze protein recruitment to the edge of the cell and reduce the effects of signal increase due to ruffling. Are there any techniques to keep the cell flat on the coverslip? thank you so much for your help!
I am currently working on design of fluorescent small molecules for various medical purposes such as selective inhibitors or imaging agents. I wonder to know if it is possible to computationally predict the fluorescence properties of a molecule? such as the fluorogenic activity of different structures or prediction of λexcitation and λemission.
Is there any software or online server available?
I'm looking to assemble a goniometer for an experiment involving adhesion/roll of blood on different materials. Effectively I need to put together a stage, where the angle can be adjusted/set and measured precisely while the material is firmly secured. As well as this I will need to be able to take photographs of the roll, so the setup should allow for lights/camera.
There are several online but they are £££. Any experience creating a similar setup appreciated! Links to components would be great.
I want to have a optical system where, I focus a beam onto the BFP of a microscope objective. Unfortunately, I always have a strong Back Reflection from the objective. Can anyone suggest me some tips to counter that?
I am trying to characterize the microstructure (localization of carbohydrates, fats, and proteins) of coconut milk powder using confocal microscopy. From the review of the available literature, I have found that fats and proteins can be non covalently labeled using fluorescent dyes. However, I am having trouble deciding the labeling protocol for the carbohydrate. Two common methods that I have seen in the papers are as follows:
1. Use antibodies or lectins conjugated with fluorophores to label carbohydrates
2. Covalent labeling of carbohydrates with FITC
If I use the first method, the signal from antibodies or lectins may interfere with the signal from protein present in the sample.
In the second method, the FITC (probe used for covalent labeling) also shows an affinity for proteins. So, I am afraid that the use of such a probe may also interfere with the protein signal (from the food sample). Is there any other probe available that I can use?
What would be the best way to label carbohydrates such that I can simultaneously image three components in the food mixture?
I want to place 2 camera lenses (eg Thorlabs MVL12M23 and MVL50M1) inside the inner vacuum can of an Oxford Kelvinox MX250 dilution cryostat. The camera lenses will be thermally connected to the helium bath and will sit at around 4.2 K. They will be brought to this temperature over the course of a few hours. I intend to set the lenses to infinity and maximum aperture, then never adjust them again. They will be used facing each other in a tandem setup, similar to this article: 10.1016/0165-0270(91)90038-2.
I am interested to know if these lenses would become unusably damaged during the cooling process, and if so, what the damage mechanisms are and how I might avoid them?
I'm a beginner to the Gstream pipeline. Please help me in understanding the importance of frame-rate in Capsfilter in this pipeline.
In my current project, the pipeline is given as follows : "tcambin ! capsfilter ! videoflip ! videoconvert ! appsink"
I assume that below code snippet hopefully sets the capsfilter pipeline for frame rate and image dimension:
" gst_caps_new_simple("video/x-raw", "width", G_TYPE_INT, size.width, "height", G_TYPE_INT, size.height, "framerate", GST_TYPE_FRACTION,4, 1,nullptr);"
Now the issue that I'm facing is by keeping the exposure time to 83ms and 4fps (As in code), I'm getting a particular image intensity, whereas by varying the frame rate from 4 to 7fps with the same exposure time, the image intensity tends to decrease.
In my understanding, the frame-rate in capsfilter should not affect image intensity unless we change exposure time in image capture, which is not happening in my case.
Please help me to understand, how does framerate impacts image intensity when exposure time is constant. Thanks in advance.
I want to implement a binary classifier (lesion yes/no) with the DeepLesion dataset. Therefore I also need ct images of healthy subjects because the DeepLesion dataset only includes images with lesions.
Thanks for your suggenstions!
We are pleased to announce the 9th International Workshop on Biomedical Image Registration, WBIR2020, hosted in Portorož, Slovenia! The workshop will be held in the Congress Centre Bernardin in Portorož, on 16 and 17 June, 2020.
The workshop brings together leading researchers in the area of biomedical image registration to present and discuss recent developments in the field, including methodological innovations and advances in the performance and validation on existing and novel applications. The workshop will include both oral and poster presentations, exciting keynote lectures, all with ample opportunities for discussion. At the social events you will enjoy the warm and relaxing Adriatic seaside along with authentic Mediterranean cuisine and excellent drinks.
IMPORTANT DATES Paper submission deadline: Jan 10, 2020 Notification of acceptance: Feb 21, 2020 Camera-ready deadline: March 20, 2020 Conference dates: June 16 and 17, 2020
AIMS AND SCOPE Submissions are invited in all areas of biomedical image registration. Topics of interest include, but are not limited to:
- Novel registration methodology: 2D/3D/4D, spatiotemporal/dynamic, pairwise / groupwise, slice-to-volume, projective, single/multi-modal, intra/inter-subject, model-based, patch-based, multi-channel, tracking
- Mathematical aspects of image registration: continuous/discrete optimization, real- time, similarity measures, diffeomorphisms, LDDMM, stationary velocity, inverse consistency, multi-scale
- Machine learning and deep learning techniques for registration: unsupervised / supervised / reinforcement learning, convolutional / recurrent / transformer networks, neural networks for feature extraction and matching, correspondence weighting and prediction, attention modeling, deformation learning, deep encoder- decoder networks
- Biomedical applications of registration: computer-assisted interventions, image- guided therapy, treatment planning/delivery, diagnosis/prognosis, atlas-based segmentation, label fusion, histopathology correlation, serial studies, pathology detection and localization, morphometry, biomechanics, image retrieval/restoration/fusion, imaging biomarkers for precision medicine, radiomics & radiogenomics, early proofs of concept
- Validation of registration: quantitative and qualitative methods, benchmarking, comparison studies, phantom studies, correlation to outcome, validation protocols and performance metrics, uncertainty estimation
All accepted full paper submissions will be published as a volume in the Springer's Lecture Notes in Computer Science (LNCS) series.
ORGANIZING COMMITTEE Ziga Spiclin, University of Ljubljana, Ljubljana, Slovenia Jamie McClelland, University College London, London, UK Jan Kybic, Czech Technical University in Prague, Prague, Czech Republic Orcun Goksel, ETH Zurich, Zurich, Switzerland
SPONSORS The WBIR 2020 is a MICCAI Society Endorsed Event (www.miccai.org).
I'm relatively new to microscopy imaging analysis so I'm seeking some help! I have z-stack images (.czi files) from zebrafish using a Zeiss LSM 880 confocal microscope at 40x water immersion objective. My advisor has suggested using the ZEN software to do a maximum intensity projection and then using orthogonal view. The images still look "messy" after conducting these steps in the ZEN Blue v3.1 software, so I'm wondering if you have any suggestions or protocols to analyze images. Ultimately, I would like to compare fluorescent intensities, myelin sheaths/olig, and/or internode length across my samples. (also- should I implement a deconvolution step?)
Thank you in advance!
We are studying organic micelles suspended in water or diesel and want to get images of them to see what they look like (an actual image, rather than size characteristics from something like a DLS). At a minimum, we want to see the micelles after formation, but it would be nice to observe their formation as well. Unfortunately, they are very susceptible to temperature changes so any low-temperature applications likely won't work. I know TEM is an option for this. Is anyone aware of any other options?
I am planning on performing expansion microscopy on relatively thick (300 um) tissue slices and doing a post-expansion stain with some nanoparticles. It seems that the expansion process should make the tissue more permeable, but I am having trouble finding a direct description in the literature which supports or goes against this intuition. Does anyone know whether or not a post-expanded tissue has greater permeability than an untreated fixed tissue sample? Note: my nanoparticles are rod shaped and have dimensions of 27x60 nm, but I could also try spherical 5 nm nanoparticles if needed.
I am able to draw different ellipse based on TOF triangulation with an active sensor network. but cant figure out how to generate image , Ideally, If I virtually mesh the entire structure, the nodes lie on the locus have 100% probability, and for the other nodes the greater the distance to the locus, the lower the probability, but how can i quantify the perception of individual node in terms of the distance between the nodes and loci established? Is there any algorithm available on Matlab, I am attaching the picture clarify my point.
I've been trying various iba1 antibodies with either Alexa 488 or 647 and am getting a lot of background and have never once seen anything close to resembling a microglia. I've tried blocking with various combinations of 0, .3 or 3.0% milk, 0, .3 or 1.0% BSA, with 4% normal donkey serum and nothing has worked.
Any suggestions would be very much appreciated. Perhaps there are better membrane-bound proteins I could stain for?
I really need some help with my protoplast media. I am trying to repeat this cycloheximide chase done in Kang 2003. They reference Tao 2005, where "transfected protoplasts were cultured overnight (14 h) in auxin-free K3 medium".
Based on my backtracking, I believe that the K3 medium is KAO'S medium No.3. from KAO et al., 1974? Does anyone know if this is correct?
What media have others tried to resuspend there protoplast in and then add drugs/reagents?
I would really really appreciate any help or advice!
I'd like to measure sarcoplasmic calcium on a whole muscle and not on isolated myofibers. Is it possible to perform a protocol for Fura-2 loading on a whole muscle and after that put the muscle into a liquid nitrogen and analyze the transverse muscle cryosections by fluorescense microscope?
I hope you are doing well.
I am working with imaging systems. I am confused about the effects of linear polarizer in such systems ( I mean how a linear polarizer can improve the resolution?) and why working with one polarization is better than two polarization in image processing systems?
For freezing down cells we use cryoprotective agents. Are there any methods by which we can study the formation of ice crystals when freezing cells/cell lines without a cryoprotective agent such as DMSO/Glycerol.
We are looking to visualize detailed morphological aspects of the membrane (e.g. size, shape, etc.), as well as the interior of the cell (e.g. N/C ratio, chromatin structure, etc.). We do not have millions of cells and therefore need an alternative to flow. Any suggestions on the best labeling results (e.g. Hoechst, DRAQ5, etc.) would be helpful.
I'm running a study in which I will inject some nanoparticles into mice and then section the lymph node and visualize it with confocal. Does anyone have the protocal for the lymph node sectioning and staining? Thanks.
I work with cell lines that were generated to express fluorescent fusion proteins from the endogenous promoter. They are rather short lived and lowly expressed.
When imaging (long term life cell imaging), I can see my proteins (only) when using high intensities, gain and ilumination times in the seconds range.
However, my cells (U-2OS) show autofluorescent dots that shine brighter than my actual signals (may be lipofuscins?, see images).
They really impair interpretation and quantification
You have any idea how to reduce those signals, e.g. by culture conditions?
Thankful for any idea.
Have anyone ever tried single protein tracking (let's say a secretory protein) but also see its relative position to other organelles such as ER and nucleus (labelled by other fluorophores)?
I read a few papers but they only track the protein without visualizing organelles. e.g. Liu et al. PNAS 2018.
P.S. I'd like to do it 3D in live mammalian cells but (I guess) I don't really need super-resolution as I just want to roughly see the localization of single proteins?
Dear All, I tried to make footage of the zooplankton with Canon G16 and a flash light with the wet macro lens in the sea. The problem is that while I am able to see individual zooplankton, it is bleary because of the movement. Will be thankful to receive any suggestions how to get better resolution of the plankton.
Also, for the plankton imaging in the laboratory conditions I was wondering if Dino Lite model AM3713TB (https://www.dino-lite.eu/index.php/en/component/k2/item/40-am3713tb) will be able to do the job?
Will be thankful to receive recommendations,
We are attempting to study actin/cytoskeletal function under different conditions in live cells. Does anyone know of an existing cell line that stably produces GFP-actin for purchase? I know that this can also be accomplished by transducing cells with viruses if you have any products in particular you recommend.
We are also ok with accomplishing this by labeling. I have tried BacMam and SiR-actin with fairly low efficacy in HeLa cells just as a trial (ideally something that works with easy to transfect and primary cells preferred). Considering trying LifeAct products but not sure if they are any better. Any recommendations on products and exactly how you applied them (number of cells, volume, inc time, concentration, etc) would be highly appreciated.
Recently, Researchers have succeeded to capture high resolution image of a molecule showing clearly its shape and chemical bonds through atomic force microscope (AFM)!!! (see attached pic.).
How could such breakthrough atomic-level imaging contribute to boost research at the interface chemistry/biology ?
I run MC simulations with MCNP6, of the imaging process in CyberKnife radiosurgery system. I want to score the scattered photon fluence in a region simulating my detector that comes from a tube that produces 120kVp.
My question is how to score in a different bin the scattered fluence that comes from different cells of interest.
I'm trying to do Photoacoustic Imaging with a 532nm laser. But i'm struggling to get signal on the oscilloscope.
I'm not sure if that is because the signal is too weak. I've tried human hair (black) and metal wire. Is there any other good material that absorbs 532nm light and generate ultrasound? The testing material should be around 100um size and will be embedded in agar.
Moreover, is all the light energy absorbed transformed to sound energy?
Hi everyone !
I am performing acute slice Ca-imaging and I would like to register the fluo rate increase on neurons in response to DHPG(
group I mGlu receptor agonist). Does somenone know if I can stimulate the same slice multiple times with DHPG ? Or does only the first stimulation is reliable ?
I obtain very variable responses but I don't know if it's correlated with the number of stimulations or if the responses are classically very variable in this experiment...
Thank you for your help
We have been sorting cell from the inner ear cochlea, and we would like to check for contaminants (the purity of our sorted cells) by staining samples of sorted cells. However, after Cytospin, the cells are so dispersed and thus hard to image or quantify.
I was wondering if there's another way of doing immunofloresence staining on sorted cells (with limited among) or if there's any cytospin funnel clips that has much smaller hole.
Thank you very much!
The lens is made for a different thermal camera, but I can obtain images. But the temperatures estimated (FLIR) are incorrect. What parameters would I need to know in order to correct this (and is it even possible to do so with some degree of accuracy)?
I hope everything goes well.
I want to be familiar with molecular dynamics and Coulomb Explosion Imaging (CEI).
Could you please explain what COLTRIMS, VMI and TOFMS do? and in which applications they are used? what are differences?
Do we choose them related to our applications? Do they depend on light sources (X-Ray, Femtosecond laser pulses, Ion impact / electron impact collision) or other things?
What are advantages and disadvantages of them?
and at the end, are there such other apparatuses like them to image the molecules?
I have three images of the same scene with a set of triple correspondences. I can calculate the trifocal tensor and recover pairwise fundamental matrices, rotation matrices, and translation vectors (up to a scale between first and second translations). This scale can be easily calculated in a noiseless case (simulation). However, as soon as even small noise is added (Gaussian, with sigma=0.1 pixel), all estimations go seriously wrong. All triples are guaranteed inliers, but even optimization techniques fail to find correct (known in simulation) scale. Does anyone know where the catch might be?
I want to use a MRI images dataset in order to detect heart failure with image processing techniques. In the beginning I should choose the kind of map I need. T1 map or T2 map, I should choose one of them.
But I don’t know what is the differences between them and which one is better for detecting heart failure.
Can anyone share some information about that?
I'm attempting to single-cell sort U2os cells into a 384-plate for imaging purposes, but my cells refuse to grow. I see no growth in any of the wells after 10+ days in +37 °C with 5% CO2. I can see a single cell has been successfully sorted into the wells, but it looks dead and there's cell debris on the bottom.
I detach the U2os cells from the bottle with PBS + 10 mM EDTA and change into FACS buffer for sorting, which is PBS + 10 mM EDTA + 10% FBS. I've pre-pipeted 100 µl of conditioned DMEM+10% FBS (1/3 ratio of used/fresh media) with Pen-Strep in the wells before sorting.
Any ideas what I could do differently? Or is there a more robust cell line that I could use, that has well defined organelles and is good for imaging.
The backscattering of electrons obviously happens with the core of the atoms or ions. If it is related to the mass I would expect an impact of protons and neutrons. If it is an impact of the charge (quite unlikely since plus and minus should attract each other) it should be proportional to the the protons only (i.e. Z, the atomic or periodic number). Nevertheless, it is not a single event since we have a practically unlimited number of interactions which should be related to the number of atoms (cores). This would bring the packing or mass density (or in first approximation the materials density) into the business. This from my present point of view very logical conclusion is in strict contradiction to experimental observations: comparing lead (density around 10g/cm³) and gold (density around 20g/cm³ ), lead has a higher backscatter coefficient. Does anybody have an idea, why the backscatter coefficient scales with Z and not with the density...or something else like a proton-density since the mass density also considers the neutrons?
I would like to use Neuron Studio in order to quantify dendrite and spine morphological features in 200 um brain sections stained with Golgi-Cox.
Neuron Studio software opens TIFF stacks derived from ND2 format through ImageJ Plug-in conversion, but doesn't trace any neurite when asked to, I think because of an apparent resolution drop (the TIFF stack looks the same as ND2 when in ImageJ, but looks low quality when in Neuron Studio).
Did anybody encounter this problem before and knows how to solve it?
Thank you in advance.
P.S. These are two examples of what I see in ImageJ (1) and in Neuron Studio (2) for the same stack.
In a modern ophthalmic setup assistants may send to the doctors images over the internet to diagnose retinal diseases. Which model do you think is the best for this aim?
SNOM combines interesting features of light microscopy and scanning microscopic methods, therefore providing high resolutions (nano structural). But there are not as many examples of it in articles as it should. I want to know the reason behind it.
I have to measure the thickness of a coating on PET fabrics.
I'm trying to use Imaging ellipsometry, but I'm realizing it is quite hard.
Thank you in advance
The 3D Bragg coherent x-ray diffractive imaging involves the measurement of rocking curve scans in the vicinity of Bragg reflections. The counting time at 3rd generation synchrontron is on the order of minutes for 200 nm objects. However, in a lot of cases the particles start to rotate under the beam.
Are there any known good ways to fixate the particles under high fluxes of x-rays (1e11 ph/µm) ?
I would like to ask for some advice about the I-Bright
Chemiluminescence Imaging System and AI680. Which has the best image and analysis software? The I-Bright camera has a better resolution but I heard the software isn´t good. Thank you.
I have an upcoming art project to draw an antioxidant molecule.
I'd like to draw the alpha-tocopherol molecule, illustrating the sub-atomic particles (nucleus and electrons) of the molecule as they would theoretically appear if we could actually visualize the electron particles orbiting around the nucleus for each atom in the molecule.
This would be a dramatized 3D representation, illustrating the sub-atomic particles in-motion rather than the static a "ball-and-stick" or "3d-space-fill" model seen in most textbooks.
However I can't find any book or program that shows the individual electron orbiting path for alpha-tocopherol. (such as the bonding orbitals)
Interconnected Smart CCTVs are integral part of Smart Transportation.
What additional information does the phase measurement in a frequency-domain imaging technique provide compared with the continuous wave technique that measures only the amplitude of the diffuse light?
I know magnetoencephalography (MEG) records magnetic fields-which are very small- produced by electrical currents in brain to map brain activities. how effective the external magnetic fields can be on the response? can we also use them (external magnetic fields) to change brains activity on a good way-such as improving memory?
I would appreciate it if someone explains the basic physical principles underlying the differences in appearance (image content, and tissue differentiation) among T1, T2, and PD weighted images.
I am looking for protein protein inteactions between a shuttle protein and nuclear hormone receptor using BIFC. When I perform BIFC with Fos and Jun I get bright signal and when I use Mutated Fos and Jun I get no signal, which indicates that my experiment is working correctly.
When I perform BIFC with my proteins of interest I get positive signal. When I perform with my nuclear receptor and Jun, I get no signal (good) but when I perform with my protein of interest and Fos I get a similar signal as my test samples.
Does anyone know the reason why this might be? The mfos/ jun combination suggests that it is not due to collisional interactions and so I am stumped as to how to approach this.
Many thanks for any assistance you can offer