issue contents

ISSN: 2053-230X

January 2008 issue

Highlighted illustration

Cover illustration: A photomontage of crystal micrographs from papers published in Acta Cryst. F in 2007. Top row: putative zinc transporter CzrB from Thermus thermophilus (Höfer et al., pp. 673-677); tetrasulfocyanine, a fluorescent probe, in complex with the Fab antibody fragment MOR03268 (Hillig et al., pp. 217-223); and the homing endonuclease I-Dmo-I in complex with its target DNA (Redondo et al., pp. 1017-1020). Middle row: an Escherichia coli tRNAGly acceptor-stem microhelix (Förster et al., pp. 46-48); BigR, a transcription repressor from Xylella fastidiosa (Barbosa et al., pp. 596-598); and PH1010 from Pyrococcus horikoshii OT3 (Shirokane et al., pp. 532-534). Bottom row: the N-terminal region of the human formin-homology protein FHOD1 (Schulte et al., pp. 878-881); the archaeal transcription termination factor NusA (Tanaka et al., pp. 69-73); and Escherichia coli WrbA in complex with its cofactor flavin mononucleotide (Wolfová et al., pp. 571-575).


Acta Cryst. (2008). F64, 1
doi: 10.1107/S1744309107066456

protein structure communications

Acta Cryst. (2008). F64, 2-7
doi: 10.1107/S1744309107065931
link to html
The structure of HsaD, a carbon–carbon bond serine hydrolase involved in steroid catabolism that is critical for the survival of M. tuberculosis inside human macrophages, has been solved by X-ray crystallography. Data were collected at the Diamond Light Source in Oxfordshire, England: this paper describes one of the first structures determined at the new synchrotron.

crystallization communications

Acta Cryst. (2008). F64, 14-18
doi: 10.1107/S1744309107057260
link to html
A procedure for microseeding into nanolitre crystallization drops is described with selected successful examples.

Acta Cryst. (2008). F64, 19-21
doi: 10.1107/S1744309107059696
link to html
E. coli SdiA was overexpressed, purified and crystallized. The crystals belonged to the hexagonal space group P6122 or P6522 and diffracted to 2.7 Å resolution.

Acta Cryst. (2008). F64, 22-24
doi: 10.1107/S1744309107060897
link to html
The sorbitol operon regulator from K. pneumoniae has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 3.2 Å.

Acta Cryst. (2008). F64, 25-28
doi: 10.1107/S174430910706160X
link to html
The high-resolution mass-spectrometric characterization, crystallization and X-ray diffraction studies of a recombinant IgE Fab fragment in complex with bovine β-lactoglobulin are reported.

Acta Cryst. (2008). F64, 29-31
doi: 10.1107/S1744309107064391
link to html
Crystals of the peroxiredoxin domain of a larger natural hybrid protein from T. maritima were obtained which diffracted to 2.9 Å resolution on a synchrotron source.

Acta Cryst. (2008). F64, 32-35
doi: 10.1107/S1744309107064615
link to html
The purification, identification, crystallization and preliminary crystallographic studies of an allergy-related protein, Pru du amandin, from P. dulcis nuts are reported.

Acta Cryst. (2008). F64, 36-38
doi: 10.1107/S1744309107065256
link to html
UlaG, the putative L-ascorbate-6-phosphate lactonase encoded by the ulaG gene from the utilization of L-ascorbate regulon in E. coli, has been cloned, overexpressed, purified using standard chromatographic techniques and crystallized in a monoclinic space group. Crystals were obtained by the sitting-drop vapour-diffusion method at 293 K. A data set diffracting to 3 Å resolution was collected from a single crystal at 100 K.

Acta Cryst. (2008). F64, 39-43
doi: 10.1107/S1744309107065372

Acta Cryst. (2008). F64, 44-46
doi: 10.1107/S1744309107065384
link to html
Human paired Ig-like type 2 receptor α (PILRα) has been expressed, purified and crystallized. A diffraction data set has been collected to 1.3 Å resolution.

Acta Cryst. (2008). F64, 47-49
doi: 10.1107/S1744309107065645
link to html
SMU.573 from S. mutans was expressed in E. coli and crystallized. The crystals belong to space group I4 and 2.5 Å resolution diffraction data were collected at an in-house chromium radiation source.

Acta Cryst. (2008). F64, 50-53
doi: 10.1107/S1744309107066122
link to html
Crystals of an active-site mutated hydantoin racemase from S. meliloti have been obtained in the presence and absence of D,L-5-isopropyl-hydantoin and characterized by X-ray diffraction.

Acta Cryst. (2008). F64, 54-57
doi: 10.1107/S1744309107066444
link to html
A new crystallization strategy: the presence of cleaved thioredoxin fusion is critical for crystallization of the estrogen nuclear receptor ligand binding domain in complex with synthetic ligands. This novel technique should be regarded as an interesting alternative for crystallization of difficult proteins.

Acta Cryst. (2008). F64, 58-61
doi: 10.1107/S1744309107066821
link to html
The cloning, expression, purification, crystallization and preliminary X-ray characterization of two protein constructs of the second type II cohesin module from A. cellulolyticus ScaB are described. Both constructs contain the native N-terminal linker, but only one of them contains the full-length 45-residue C-terminal linker; the other contains a five-residue segment of this linker.

addenda and errata

Acta Cryst. (2008). F64, 62
doi: 10.1107/S1744309107065566
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