issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

March 2016 issue

Highlighted illustration

Cover illustration: The X-ray structure of the thymidine phosphorylase from Salmonella typhimurium in complex with uridine (p. 224).

research communications


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The structure of human growth differentiation factor 11 (GDF11) determined to a resolution of 1.50 Å reveals subtle conformational differences when compared with the previously determined structure of human myostatin (GDF8) while maintaining a highly similar quaternary architecture.


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A putative exopolyphosphatase (PPX) from Z. mobilis (ZmPPX) was expressed, purified and crystallized. PPX enzymes regulate intracellular inorganic polyphosphate levels in microbial cells in response to external stresses. N-terminal truncation of ZmPPX based on primary-sequence analysis resulted in an improvement in diffraction from 3.3 to 1.8 Å resolution.

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The crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase, a component of the shikimate pathway, was determined during its evaluation as a target for new antimicrobials effective against multidrug-resistant, extensively drug-resistant and pan-drug-resistant A. baumannii. This enzyme is essential for the growth and survival of this clinically important pathogen during host infection.

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Molecular replacement and noncrystallographic symmetry averaging were used to detwin a data set affected by perfect hemihedral twinning. The noncrystallographic symmetry averaging of the electron-density map corrected errors in the detwinning introduced by the differences between the molecular-replacement model and the crystallized structure.

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The crystal structure of an N-terminally truncated form of leucine zipper II (LZII) of JIP3 alone shows an unexpected antiparallel arrangement. This study draws attention to the fact that LZII of JIP3/JIP4 is a versatile structural motif, modifications of which can impact partner recognition and thus biological functions.

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Recombinant C1ORF123 protein from H. sapiens was overexpressed, purified to homogeneity and crystallized. Diffraction data were collected for X-ray crystallographic analysis.

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The crystal structure of the FhuD protein from S. pseudintermedius was determined at 1.6 Å resolution. The structure displays a canonical class III solute-binding protein fold in a closed conformation, revealing a ligand-binding site suitable for the accommodation of siderophore ligands, here occupied by a polyethylene glycol molecule.

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The crystallization of perdeuterated P. aeruginosa peptidyl-tRNA hydrolase 1 and initial neutron diffraction data collection are reported.

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Structures of thymidine phosphorylase from S. typhimurium were determined in the unliganded state and in complexes with thymidine and uridine. The structural origins of the substrate specificity were found.

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The purification, crystallization and initial X-ray crystallographic studies of the N-terminal and M domains of the α-catenin homologue HMP-1 from C. elegans are described.

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The cloning, expression, purification and crystallization of the CH domain of the plant-specific kinesin GhKCH2 is reported.

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The crystal structure of MtaL shows that conformational changes are needed for binding to mushroom tyrosinase and reveals a putative carbohydrate-binding site that may be associated with glycoreceptor activity.

addenda and errata




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