Open AccessProtein preparation and preliminary X‐ray crystallographic analysis of a putative glucosamine 6‐phosphate deaminase from Streptococcus mutants
Author(s) -
Hu GuanJing,
Li LanFen,
Li Dan,
Liu Cong,
Wei ShiCheng,
Liang YuHe,
Su XiaoDong
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107040304
Subject(s) - fusion protein , microbiology and biotechnology , glucosamine , escherichia coli , crystallography , chemistry , mutant , gene , biology , biochemistry , recombinant dna
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 Å resolution and belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 53.83, b = 82.13, c = 134.70 Å.