Open AccessCrystallization and preliminary X‐ray analysis of the receiver domain of a putative response regulator, BPSL0128, from Burkholderia pseudomallei
Author(s) -
Abd Aziz Abd Ghani,
Sedelnikova Svetlana E.,
Ruzheinikov Sergey N.,
Thorpe Simon,
Mohamed Rahmah,
Nathan Sheila,
Rafferty John B.,
Baker Patrick J.,
Rice David W.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112025791
Subject(s) - burkholderia pseudomallei , regulator , crystallization , escherichia coli , resolution (logic) , peg ratio , strain (injury) , response regulator , gene , biology , chemistry , microbiology and biotechnology , crystallography , bacteria , bacterial protein , genetics , organic chemistry , finance , anatomy , artificial intelligence , computer science , economics
bpsl0128 , a gene encoding a putative response regulator from Burkholderia pseudomallei strain D286, has been cloned into a pETBLUE‐1 vector system, overexpressed in Escherichia coli and purified. The full‐length protein is degraded during purification to leave a fragment corresponding to the putative receiver domain, and crystals of this protein that diffracted to beyond 1.75 Å resolution have been grown by the hanging‐drop vapour‐diffusion technique using PEG 6000 as the precipitant. The crystals belonged to one of the enantiomorphic pair of space groups P 3 1 21 and P 3 2 21, with unit‐cell parameters a = b = 65.69, c = 105.01 Å and either one or two molecules in the asymmetric unit.