Published December 23, 2010 | Version v1
Journal article

Crystallization and preliminary X-ray crystallographic analysis of the short-chain dehydrogenase/reductase-type DDB-G0291732 protein from Dictyostelium discoideum

  • 1. Laboratory of Biophysics, School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742 (Korea, Republic of)

Description

In order to investigate its structure and function, the NmrA-like short-chain dehydrogenase/reductase-type DDB-G0291732 protein from D. discoideum was expressed, purified and crystallized. X-ray diffraction analysis is reported to a resolution of 1.65 Å. The DDB-G0291732 gene product from Dictyostelium discoideum, which is a NmrA-like protein that belongs to the short-chain dehydrogenase/reductase superfamily but shows deviations in conserved sequence regions, has been crystallized by the hanging-drop vapour-diffusion method at 295 K. A 1.65 Å resolution data set was collected using synchrotron radiation. The crystals of DDB-G0291732 protein belonged to space group P21, with unit-cell parameters a = 38.5, b = 63.7, c = 56.0 Å, β = 91.7°. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 38.1%

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309110046932; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079983

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
67
Journal Issue
Pt 1
Journal Page Range
p. 98-100
ISSN
1744-3091
CODEN
ACSFCL

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2011
Notes
PMCID: PMC3079983; PMID: 21206035; PUBLISHER-ID: pu5312; OAI: oai:pubmedcentral.nih.gov:3079983