issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

February 2010 issue

Highlighted illustration

Cover illustration: A new crystal form of human diamine oxidase (McGrath et al., p. 136).

editorial


Acta Cryst. (2010). F66, 112
doi: 10.1107/S1744309110001326

structural communications


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The crystal structure of bovine pancreatic ribonuclease A in complex with uridine 5′-monophosphate was determined at 1.60 Å resolution. The uridine lies in the pyrimidine-specific binding site of the enzyme, with the phosphate group extended into the solvent without interacting with the protein.

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The crystal structure of B. amyloliquefaciens α-amylase (BAA) at 1.4 Å resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family.

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The crystal structure of uracil-DNA N-glycosylase from Vibrio cholerae has been determined at 1.5 Å, and used for mapping temperature adaptation.

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The structure of human diamine oxidase has been refined to 2.1 Å resolution in space group C2221.

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A 1.9 Å resolution crystal structure of the isolated kinase domain from the α2 subunit of human AMPK, the first from a multicellular organism, is presented.

crystallization communications


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The expression, purification and crystallization of the collagen-binding region of the E. rhusiopathiae surface protein RspB is described. The crystals diffracted to 2.2 Å resolution using synchrotron radiation.

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In this study, D,D-heptose-1,7-bisphosphate phosphatase has been cloned, expressed, purified and crystallized.

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Recombinant P. somniferum salutaridine reductase (SalR) was purified and crystallized with NADPH using the hanging-drop vapor-diffusion method. Crystals of the SalR–NADPH complex diffracted X-rays to a resolution of 1.9 Å.

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The antitoxin Phd from the phd/doc operon of bacteriophage P1 was crystallized in two distinct crystal forms.

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The purification, crystallization and preliminary X-ray diffraction analysis of a surface-associated antigen from the major human hookworm N. americanus is presented.

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The minor pilin FctB from S. pyogenes strain 90/306S was expressed in E. coli, purified and crystallized. The hexagonal FctB crystals diffracted to 2.9 Å resolution.


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1,3-Propanediol dehydrogenase (Aq_1145) from A. aeolicus VF5 has been overexpressed, purified and crystallized. The crystals diffracted to 2.4 Å resolution.

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Recombinant glycine decarboxylase from Synechocystis sp. PCC 6803 was expressed in E. coli and purified to homogeneity. Crystals were obtained that diffracted to 2.1 Å resolution using synchrotron radiation.

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The production and crystallization of the human DEAD box polypeptide 5 are reported. A 2.7 Å native diffraction data set has been obtained.

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Crystals of the Grb2 SH2 domain in complex with a phosphotyrosyl peptide corresponding to residues 921–930 of focal adhesion kinase (FAK) have been obtained using the sitting-drop vapour-diffusion technique. Data have been collected to 2.49 Å resolution.

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In this study, the mature form of SPN48 was overexpressed in Escherichia coli and purified. The purified SPN48 protein was crystallized using 14% polyethylene glycol 8000 and 0.1 M 2-(N-morpho­lino)ethanesulfonic acid pH 6.0 as the precipitant. The crystals diffracted X-rays to 2.1 Å resolution and were suitable for structure determination.

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VSP1 from Arabidopsis thaliana was expressed in E. coli, purified and crystallized. X-ray diffraction data were collected to 1.9 Å resolution.

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Psu, a unique 21 kDa protein from bacteriophage P4, is a non-essential capsid-decoration protein that inhibits Rho-dependent termination specifically and efficiently both in vivo and in vitro. Psu has been crystallized using PEG as precipitant and the crystals diffracted to 2.3 Å resolution.

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E. cuniculi Iws1, which acts in eukaryotic transcription and mRNA processing and export, has been crystallized and data have been collected to 2.5 Å resolution.

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The FAF1 UBX domain was crystallized. X-ray diffraction data were collected to 3.00 Å resolution and the crystals belonged to space group F4132.

addenda and errata


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