- James Taylor added an answer:Is it possible to build a reliable model of a protein ternary complex from sequence data?I have four proteins A, B, C and D. A is a transmembrane receptor and its the substrate that gets phosphorylated in its cytosolic domain. B is the kinase, therefore, Mg++ and ATP dependent. B also depends on C and D for its activity. There might as well be a domain swapping between B and C. Is it at all possible to build a reliable model of the ternary complex of BCD? I only have the sequence data. Direct structural information of these proteins is not available.Can you purify the complex?Following
- Krishna Raut added an answer:Can somebody advise how to find out find out I(0) value from I(q) vs q2 plot using the relation I(q)=I(0)exp(-q2Rg2/3) in origin?Seeking a forward scattering intensity value I(0) from the plot of I(q) vs q2Thank you Fernando for your valuable suggestion.Following
- Mervi T Hyvönen added an answer:Cross-linking RNA and protein.What is the most efficient and easiest way to specifically cross-link a protein to its RNA substrate?For trypsinized cells, I use 1% formaldehyde/PBS at rt for 15-30 min, after which I quench with 125 mM glycine, centrifuge and wash with PBS.Following
About Small-Angle X-ray Scattering (SAXS)
Small-angle X-ray scattering (SAXS) is a small-angle scattering (SAS) technique where the elastic scattering of X-rays by a sample which has inhomogeneities in the nm-range, is recorded at very low angles (typically 0.1 - 1). This angular range contains information about the shape and size of macromolecules, characteristic distances of partially ordered materials, pore sizes, and other data. SAXS is capable of delivering structural information of macromolecules between 5 and 25 nm, of repeat distances in partially ordered systems of up to 150 nm.