Acta Crystallographica Section F Structural Biology and Crystallization Communications Journal Impact Factor & Information

Publisher: International Union of Crystallography, International Union of Crystallography

Journal description

Acta Crystallographica Section F Structural Biology and Crystallization Communications aims to provide a home for communications on the crystallization and structure determination of biological macromolecules.

Current impact factor: 0.57

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 0.568
2012 Impact Factor 0.552
2011 Impact Factor 0.506
2010 Impact Factor 0.563
2009 Impact Factor 0.551
2008 Impact Factor 0.606
2007 Impact Factor 0.645

Impact factor over time

Impact factor

Additional details

5-year impact 0.49
Cited half-life 3.50
Immediacy index 0.22
Eigenfactor 0.01
Article influence 0.18
Website Acta Crystallographica Section F website
Other titles Acta crystallographica. Section F, Structural biology and crystallization communications, Structural biology and crystallization communications online, (IUCr) structural biology and crystallization communications online
ISSN 1744-3091
OCLC 56932079
Material type Document, Newspaper, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

International Union of Crystallography

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • On author's personal website, employer's website, employer's repository, or subject-based repository
    • Publisher's version/PDF may be used (authorised electronic re-print) (preferred)
    • Publisher's version/PDF (authorised electronic re-print) on PubMed Central and related servers
    • Pre-print must acknowledge submission to journal
    • Must link to publisher version on IUCr server
    • Published source must be acknowledged with citation
    • Publisher last contacted on 23/04/2014
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Sialidases and trans-sialidases play important roles in the life cycles of various microorganisms. These enzymes can serve nutritional purposes, act as virulence factors or mediate cellular interactions (cell evasion and invasion). In the case of the protozoan parasite Trypanosoma vivax, trans-sialidase activity has been suggested to be involved in infection-associated anaemia, which is the major pathology in the disease nagana. The physiological role of trypanosomal trans- sialidases in host–parasite interaction as well as their structures remain obscure. Here, the production, purification and crystallization of a recombinant version of T. vivax trans-sialidase 1 (rTvTS1) are described. The obtained rTvTS1 crystals diffracted to a resolution of 2.5 A ̊ and belonged to the orthorhombic space group P212121, with unit-cell parameters a = 57.3, b = 78.4, c = 209.0 A ̊ .
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 05/2015; 71(Pt 5):577-585. DOI:10.1107/S2053230X15002496
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    ABSTRACT: Drosophila Down syndrome cell adhesion molecule 1 (Dscam1) plays a critical role in neural development. It can potentially form 38 016 isoforms through alternative RNA splicing, and exhibits isoform-specific homophilic interaction through three variable Ig domains (Ig2, Ig3 and Ig7). The diversity and homophilic interaction are essential for its functions. Ig7 has 33 isoforms and is the most variable among the three variable Ig domains. However, only one isoform of Ig7 (isoform 30) has been structurally determined to date. Here, two isoforms of Dscam1 Ig7 (isoforms 5 and 9; Ig75 and Ig79) were produced and crystallized. Diffraction data from Ig75 and Ig79 crystals were processed to resolutions of 1.95 and 2.37 Å, respectively. Comparison of different Dscam1 Ig7 isoforms will provide insight into the mechanism of its binding specificity.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):330-2. DOI:10.1107/S2053230X15002897
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    ABSTRACT: The arginine repressor (ArgR) is a transcriptional regulator which regulates genes encoding proteins involved in arginine biosynthesis and the arginine catabolic pathway. ArgR from the alkaliphilic bacterium Bacillus halodurans was cloned and overexpressed in Escherichia coli. ArgR (Bh2777) from B. halodurans is composed of 149 amino-acid residues with a molecular mass of 16 836 Da. ArgR was crystallized at 296 K using 1,2-propanediol as a precipitant. Crystals of N-terminally His-tagged ArgR were obtained by the sitting-drop vapour-diffusion method. Dehydrated crystals showed a dramatic improvement in diffraction quality and diffracted to 2.35 Å resolution. The crystals belonged to the cubic space group I23, with unit-cell parameters a = b = c = 104.68 Å. The asymmetric unit contained one monomer of ArgR, which generates a trimer by the threefold axis of the space group, giving a crystal volume per mass (VM) of 2.98 Å(3) Da(-1) and a solvent content of 56.8%.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):291-4. DOI:10.1107/S2053230X15000904
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    ABSTRACT: Acetophenone reductase (APRD) from Geotrichum candidium NBRC 4597 was crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as a precipitant. The crystal belonged to space group P6522, with unit-cell parameters a = b = 104.5, c = 273.7 Å, and diffracted to 2.6 Å resolution. Phasing using the single-wavelength anomalous diffraction method was successful. Model building and crystallographic refinement are in progress.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):320-3. DOI:10.1107/S2053230X15002265
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    ABSTRACT: Crystallization phase diagrams are frequently used to conceptualize the phase relations and also the processes taking place during the crystallization of macromolecules. While a great deal of freedom is given in crystallization phase diagrams owing to a lack of specific knowledge about the actual phase boundaries and phase equilibria, crucial fundamental features of phase diagrams can be derived from thermodynamic first principles. Consequently, there are limits to what can be reasonably displayed in a phase diagram, and imagination may start to conflict with thermodynamic realities. Here, the commonly used `crystallization phase diagrams' are derived from thermodynamic excess properties and their limitations and appropriate use is discussed.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):247-60. DOI:10.1107/S2053230X1500374X
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    ABSTRACT: Caprin-1 is an RNA-binding protein which plays critical roles in several important biological processes, including cellular proliferation, the interferon-mediated antiviral innate immune response, the maintenance of synaptic plasticity and the formation of RNA stress granules. Caprin-1 has been implicated in the pathogenesis of several human diseases, including osteosarcoma, breast cancer, viral infections, hearing loss and neurodegenerative disorders. Despite the emerging biological and physiopathological significance of Caprin-1, no structural information is available for this protein. Moreover, Caprin-1 does not have sequence similarity to any other protein with a known structure. It is therefore expected that structural studies will play a particularly crucial role in revealing the functional mechanisms of Caprin-1. Here, a protein fragment of human Caprin-1 consisting of residues 112-260 was expressed, purified and crystallized. Native and Se-SAD data sets were collected to resolutions to 2.05 and 2.65 Å, respectively, in different space groups.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):324-9. DOI:10.1107/S2053230X15002642
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    ABSTRACT: The type VI secretion system (T6SS) is a machine evolved by Gram-negative bacteria to deliver toxin effectors into target bacterial or eukaryotic cells. The T6SS is functionally and structurally similar to the contractile tail of the Myoviridae family of bacteriophages and can be viewed as a syringe anchored to the bacterial membrane by a transenvelope complex. The membrane complex is composed of three proteins: the TssM and TssL inner membrane components and the TssJ outer membrane lipoprotein. The TssM protein is central as it interacts with both TssL and TssJ, therefore linking the membranes. Using controlled trypsinolysis, a 32.4 kDa C-terminal fragment of enteroaggregative Escherichia coli TssM (TssM32Ct) was purified. A nanobody obtained from llama immunization, nb25, exhibited subnanomolar affinity for TssM32Ct. Crystals of the TssM32Ct-nb25 complex were obtained and diffracted to 1.9 Å resolution. The crystals belonged to space group P64, with unit-cell parameters a = b = 95.23, c = 172.95 Å. Molecular replacement with a model nanobody indicated the presence of a dimer of TssM32Ct-nb25 in the asymmetric unit.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):266-71. DOI:10.1107/S2053230X15000709
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    ABSTRACT: Two crystal forms of Escherichia coli tryptophanase (tryptophan indole-lyase, Trpase) were obtained under the same crystallization conditions. Both forms belonged to the same space group P43212 but had slightly different unit-cell parameters. The holo crystal form, with pyridoxal phosphate (PLP) bound to Lys270 of both polypeptide chains in the asymmetric unit, diffracted to 2.9 Å resolution. The second crystal form diffracted to 3.2 Å resolution. Of the two subunits in the asymmetric unit, one was found in the holo form, while the other appeared to be in the apo form in a wide-open conformation with two sulfate ions bound in the vicinity of the active site. The conformation of all holo subunits is the same in both crystal forms. The structures suggest that Trpase is flexible in the apo form. Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):286-90. DOI:10.1107/S2053230X15000850
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    ABSTRACT: Aurora A is a Ser/Thr protein kinase that functions in cell-cycle regulation and is implicated in cancer development. During mitosis, Aurora A is activated by autophosphorylation on its activation loop at Thr288. The Aurora A catalytic domain (amino acids 122-403) expressed in Escherichia coli autophosphorylates on two activation-loop threonine residues (Thr288 and Thr287), whereas a C290A,C393A double point mutant of the Aurora A catalytic domain autophosphorylates only on Thr288. The structure of the complex of this mutant with ADP and magnesium was determined to 2.1 Å resolution using molecular replacement. This is an improvement on the existing 2.75 Å resolution structure of the equivalent wild-type complex. The structure confirms that single phosphorylation of the activation loop on Thr288 is insufficient to stabilize a `fully active' conformation of the activation loop in the absence of binding to TPX2.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):315-9. DOI:10.1107/S2053230X15002290
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    ABSTRACT: The mammalian haem peroxidase superfamily consists of myeloperoxidase (MPO), lactoperoxidase (LPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). These enzymes catalyze a number of oxidative reactions of inorganic substrates such as Cl(-), Br(-), I(-) and SCN(-) as well as of various organic aromatic compounds. To date, only structures of MPO and LPO are known. The substrate-binding sites in these enzymes are located on the distal haem side. Propylthiouracil (PTU) is a potent antithyroid drug that acts by inhibiting the function of TPO. It has also been shown to inhibit the action of LPO. However, its mode of binding to mammalian haem peroxidases is not yet known. In order to determine the mode of its binding to peroxidases, the structure of the complex of LPO with PTU has been determined. It showed that PTU binds to LPO in the substrate-binding site on the distal haem side. The IC50 values for the inhibition of LPO and TPO by PTU are 47 and 30 µM, respectively. A comparision of the residues surrounding the substrate-binding site on the distal haem side in LPO with those in TPO showed that all of the residues were identical except for Ala114 (LPO numbering scheme), which is replaced by Thr205 (TPO numbering scheme) in TPO. A threonine residue in place of alanine in the substrate-binding site may affect the affinity of PTU for peroxidases.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):304-10. DOI:10.1107/S2053230X15001806
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    ABSTRACT: β-Catenin is a multifunctional protein involved in both cell adhesion and Wnt signaling in metazoans. The nematode Caenorhabditis elegans is unusual in that it expresses four β-catenin paralogs with separate functions. C. elegans HMP-2 participates in cell adhesion but not in Wnt signaling, so structural and biochemical studies of this protein will help in understanding its unusual specialization and the evolution of β-catenin. HMP-2 was expressed, purified and crystallized in two different salt conditions. Crystals grown from a sodium formate condition diffracted to a resolution of 2 Å and belonged to space group C2, with unit-cell parameters a = 165.2, b = 39.0, c = 101.1 Å, β = 116.7°. Crystals obtained from a lithium sulfate condition diffracted to 3 Å resolution and belonged to space group P43, with unit-cell parameters a = b = 85.3, c = 138.7 Å. Diffraction data were collected and processed from both crystal forms and the structure was solved by molecular replacement. Model refinement is in progress.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):272-6. DOI:10.1107/S2053230X15000643
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    ABSTRACT: Myotubularin-related protein 1 is a phosphatase that dephosphorylates phospholipids such as phosphatidylinositol 3-phosphate or phosphatidylinositol 3,5-bisphosphate. In this study, human MTMR1 was overexpressed in Escherichia coli, purified and crystallized at 277 K using polyethylene glycol 20 000 as a precipitant. Diffraction data were collected to 2.0 Å resolution using synchrotron radiation. The crystals belonged to space group P1, with unit-cell parameters a = 67.219, b = 96.587, c = 97.581 Å, α = 87.597, β = 86.072, γ = 77.327°. Assuming the presence of four molecules in the asymmetric unit, the calculated Matthews coefficient value was 2.61 Å(3) Da(-1) and the corresponding solvent content was 52.9%.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):261-5. DOI:10.1107/S2053230X15000606
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    ABSTRACT: The crystal structure of the aminopeptidase APDkam589 from the thermophilic crenarchaeon Desulfurococcus kamchatkensis was determined at a resolution of 3.0 Å. In the crystal, the monomer of APDkam589 and its symmetry-related monomers are densely packed to form a 12-subunit complex. Single-particle electron-microscopy analysis confirms that APDkam589 is present as a compact dodecamer in solution. The APDkam589 molecule is built similarly to the molecules of the PhTET peptidases, which have the highest sequence identity to APDkam589 among known structures and were isolated from the more thermostable archaeon Pyrococcus horikoshii. A comparison of the interactions of the subunits in APDkam589 with those in PhTET1, PhTET2 and PhTET3 reveals that APDkam589 has a much lower total number of salt bridges, which correlates with the lower thermostability of APDkam589. The monomer of APDkam589 has six Trp residues, five of which are on the external surface of the dodecamer. A superposition of the structure of APDkam589 with those having a high sequence similarity to APDkam589 reveals that, although the positions of Trp45, Trp252 and Trp358 are not conserved in the sequences, the spatial locations of the Trp residues in these models are similar.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 03/2015; 71(Pt 3):277-85. DOI:10.1107/S2053230X15000783