issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

September 2006 issue

Highlighted illustration

Cover illustration: The SH3 domain of human osteoclast-stimulating factor at atomic resolution (p. 844).

protein structure communications


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The structure of recombinant T. brucei UDP-galactose-4′-epimerase cocrystallized with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-α-D-galactose has been determined at medium resolution. Comparisons with structures of human and E. coli UDP-galactose-4′-epimerase–ligand complexes reveal that the hexose moieties are able to adopt different orientations in the active site.

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The X-ray crystallographic analysis of anti-FLAG M2 Fab is reported and the implications of the structure on FLAG epitope binding are described as a first step in the development of a tool for the structural and biophysical study of membrane proteins.

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Mutation of Tyr94 of E. coli thymidylate synthase to phenylalanine leads to a protein with kcat reduced by a factor of 400. The Y94F structure is essentially identical to the wild-type structure, which is consistent with a catalytic role for the phenolic OH.

Acta Cryst. (2006). F62, 844
doi: 10.1107/S1744309106030004
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The crystal structure of the SH3 domain of human osteoclast-stimulating factor has been determined and refined to the ultrahigh resolution of 1.07 Å. The structure at atomic resolution provides an accurate framework for structure-based design of its inhibitors.

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The structure of an uncomplexed form of α-amylase from B. halmapalus is compared with a form in which maltose, glucose and a nonasaccharide derived from acarbose and maltose are bound.

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The crystal structure of the stand-alone RAM domain from T. thermophilus HB8 has been determined at 2.4 Å resolution. The structure revealed that five dimers are arranged to form a ring.

crystallization communications


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A construct consisting of residues 10–310 of mature BipD, a component of the B. pseudomallei type III secretion system, has been crystallized. Native BipD crystals and SeMet and K2PtCl4 derivative crystals have undergone preliminary crystallographic analysis.

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IpaD, the putative needle-tip protein of the S. flexneri type III secretion system, has been crystallized in a variety of crystal forms using in-drop proteolysis. Native and selenomethionine-labelled data collection and preliminary analyses are reported.

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A 24 kDa protein was purified from the seeds of L. sativus by ammonium sulfate fractionation and ion-exchange chromatography. Crystals were obtained by the hanging-drop vapour-diffusion method.

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The CRP/FNR family transcription factor from M. tuberculosis H37Rv has been crystallized in space group P212121 in the absence of cAMP. The crystals show the presence of a dimeric molecule in the asymmetric unit.

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The C-terminal 440 amino acids of the NS3 protein from Kunjin virus (Flaviviridae) code for a helicase. The protein has been overexpressed and crystallized. Characterization of the isolated monoclinic crystal form and diffraction data (at 3.0 Å resolution) are presented, together with a preliminary molecular-replacement solution.


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Crystals of S. islandicus filamentous virus (SIFV) protein 14 have been grown at 293 K. Crystals belong to space group P6222 or P6422 and diffract to a resolution of 2.95 Å.

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PhzM, an S-adenosylmethionine-dependent methyltransferase enzyme that catalyzes a reaction involved in the biosynthesis of pyocyanin in P. aeruginosa, was cloned, overexpressed and crystallized. Data collection from native and selenomethionine-labelled crystals is reported.

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Two S. agalactiae proteins, the inorganic pyrophosphatase and the serine/threonine phosphatase, were crystallized and diffraction data were collected and processed from these crystals. The data from the two protein crystals extended to 2.80 and 2.65 Å, respectively.

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The periplasmic stress protein RseB from E. coli was cloned, expressed and crystallized. Crystallographic data are presented and structure solution using the multiple isomorphous replacement approach (MIR) is in progress.

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Pentaketide chromone synthase from A. arborescens has been overexpressed in E. coli, purified and crystallized. Diffraction data have been collected to 1.6 Å.

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Crystallization of and preliminary crystallographic studies on an active-site mutant of pro-Tk-subtilisin from the hyperthermophilic archaeon T. kodakaraensis were performed.

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The C-terminal catalytic domain of P. multocida toxin, which is the virulence factor of the organism in P. multocida, has been expressed, purified and subsequently crystallized using the sitting-drop vapour-diffusion technique.

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The SecA ATPase from T. thermophilus was cloned, expressed, purified and crystallized. Complete diffraction data sets were collected for two crystal forms at 2.8 and 3.5 Å resolution, respectively. Determination of the structure is now in progress.

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The peptidyl-tRNA hydrolase from M. tuberculosis has been crystallized in three closely related forms, two orthorhombic and one monoclinic, and X-ray diffraction data have been collected from them.


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Glutathionylated glutaredoxin Grx1p from yeast was crystallized, along with a yellow fluorescent protein–glutaredoxin fusion protein.

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In this study, the catalytic domain of rat protein tyrosine phosphatase η was produced in Escherichia coli in soluble form and purified to homogeneity. Crystals were obtained by the hanging-drop vapour-diffusion method.

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Human synaptotagmin C2A-C2B has been expressed as a glutathione-S-transferase fusion protein in Escherichia coli. The purification, crystallization and preliminary X-ray analysis of this protein are reported here.

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Glucose-1-phosphate uridylyltransferase (UgpG) from S. elodea ATCC 31461 has been expressed, purified and crystallized. Seven crystal forms were obtained and characterized to a maximum resolution of 2.65 Å.

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The phosphofructokinase-2 enzyme from E. coli was crystallized in its tetrameric inhibited form. This is the only member of the ribokinase family known to suffer a transition from dimer to tetramer in response to the allosteric binding of MgATP.

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Crystals of the C-terminal 10 kDa lid subdomain from the C. elegans chaperone Hsp70 have been obtained that diffract X-rays to ∼3.5 Å and belong to space group I212121. Analysis of X-ray data and initial heavy-atom phasing reveals 24 monomers in the asymmetric unit related by 432 non-crystallographic symmetry.
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