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: 0.53

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 0.527
2013 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 0.45
Cited half-life 4.00
Immediacy index 0.30
Eigenfactor 0.00
Article influence 0.17
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: Mycobacterium tuberculosis has multiple σ factors which enable the bacterium to reprogram its transcriptional machinery under diverse environmental conditions. σJ, an extracytoplasmic function σ factor, is upregulated in late stationary phase cultures and during human macrophage infection. σJ governs the cellular response to hydrogen peroxide-mediated oxidative stress. σJ differs from other canonical σ factors owing to the presence of a SnoaL_2 domain at the C-terminus. σJ crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 133.85, c = 75.08 Å. Diffraction data were collected to 2.16 Å resolution on the BM14 beamline at the European Synchrotron Radiation Facility (ESRF).
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 07/2015; 71(8). DOI:10.1107/S2053230X15009577
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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: 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; Ig7 5 and Ig7 9 ) were produced and crystallized. Diffraction data from Ig7 5 and Ig7 9 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: 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 P 4 3 2 1 2 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