issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

April 2015 issue

Highlighted illustration

Cover illustration: Structure of the omalizumab Fab (Jensen et al., p. 419).

IYCr crystallization series


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Growing large-volume crystals are necessary and important for neutron macromolecular crystallography. Experimental strategies, techniques and theoretical considerations for protein crystal growth are reviewed.

research communications


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The crystal structure of human P-cadherin EC1-EC2 in a closed conformation is reported at 1.62 Å resolution, showing a double conformation of Trp2 in the binding pocket and a novel monomeric packing arrangement.

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The crystal structure of fructosyl peptide oxidase from E. terrenum was determined at 1.9 Å resolution. This is the first structure of a group I FPOD that prefers α-fructosyl peptide substrates.

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A neutralizing Fab antibody fragment directed against the Wnt antagonist sclerostin was crystallized and its structure was determined by molecular replacement.

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In this study, MtaN-1 from A. hydrophila was successfully expressed and purified, and crystals in complex with the substrate SAH were obtained and diffracted to a resolution of 1.4 Å.

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A GH12 endoglucanase from A. aculeatus F-50 was expressed in P. pastoris, crystallized and diffracted to a resolution of 1.6 Å.

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HutB from V. cholerae has been cloned, overexpressed, purified and crystallized in a monomeric form. Crystals belonging to space group P43212 produced diffraction data to 2.4 Å resolution.

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Mutants of Turnip yellow mosaic virus protease/ubiquitin hydrolase designed to prevent self-recognition were produced and crystallized as monomers.

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Psb32 from T. elongatus was expressed using a novel vector library for the generation of superfolder fluorescent fusion proteins. X-ray diffraction data were collected to a resolution of 2.3 Å from a crystal belonging to space group P6122.


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The therapeutic antibody omalizumab inhibits the binding of IgE to its receptors. Two crystal structures of the omalizumab Fab fragment have been determined at 1.9 and 3.0 Å resolution.

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V. harveyi β-N-acetylglucosaminidase (VhGlcNAcase) is a glycoside hydrolase that degrades chitooligosacharides, yielding N-acetylglucosamine as the final product. Single crystals of wild-type and D437A-mutant VhGlcNAcase were grown and diffracted to resolutions of 2.37 and 2.60 Å, respectively.

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The phosphatase domain PA3346PD of the response regulator PA3346 from P. aeruginosa has been overexpressed, purified and crystallized by the sitting-drop vapour-diffusion method.

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The 800 kDa complex of the human Rod, Zwilch and ZW10 proteins (the RZZ complex) was reconstituted in insect cells, purified, crystallized and subjected to preliminary X-ray diffraction analysis.

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This article reports the co-crystal structure of the mouse ARG catalytic domain with dasatinib, a tyrosine kinase inhibitor used for the treatment of leukemia.

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The structure of dihydrodipicolinate synthase from B. thetaiotaomicron has been determined. The overall structure is described and compared with related structures.

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Analytical ultracentrifugation studies and crystallization experiments have been performed on the chloroplast envelope quinone oxydoreductase homologue (ceQORH). Diffracting crystals of ceQORH have been obtained and X-ray diffraction data were collected at 2.34 Å resolution.

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Four ficin (iso)forms from F. carica latex were isolated and crystallized. For each form, at least one crystal form was obtained that diffracted to a resolution of at least 1.60 Å.

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The cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of AerF from M. aeruginosa, which is a putative reductase that participates in the biosynthetic pathway of the 2-carboxy-6-hydroxyoctahydroindole moiety of aeruginosin, are reported.

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The cyanate hydratase CynS from S. proteamaculans was crystallized serendipitously during screens for a eukaryotic complex. Here, its crystal structure is described at 2.1 Å resolution.

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The membrane protein NDH-II from the human pathogen S. aureus was produced in E. coli, purified and crystallized. The crystals belonged to the orthorhombic space group P212121 and diffracted to 3.32 Å resolution; the structure was determined by molecular replacement.
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