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Protein preparation and preliminary X-ray crystallographic analysis of a putative glucosamine 6-phosphate deaminase from Streptococcus mutants

By Guan-Jing Hu, Lan-Fen Li, Dan Li, Cong Liu, Shi-Cheng Wei, Yu-He Liang and Xiao-Dong Su

Abstract

The SMU. 636 protein from Streptococcus mutans is a putative glucosamine 6-phosphate deaminase with 233 residues. The smu. 636 gene was PCR-amplified from S. mutans genomic DNA and cloned into the expression vector pET-28a(+). The resultant His-tagged fusion protein was expressed in Escherichia coli and purified to homogeneity in two steps. Crystals of the fusion protein were obtained by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.4 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.83, b = 82.13, c = 134.70 angstrom.http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000249154300025&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701Biochemical Research MethodsBiochemistry & Molecular BiologyBiophysicsCrystallographySCI(E)PubMed1ARTICLEPt 9809-8116

Topics: SEQUENCE
Publisher: acta crystallographica section f structural biology and crystallization communications
Year: 2007
DOI identifier: 10.1107/S1744309107040304
OAI identifier: oai:localhost:20.500.11897/198112
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