Open AccessCloning, purification, crystallization and preliminary X‐ray analysis of the Burkholderia pseudomallei L1 ribosomal protein
Author(s) -
Abd Aziz Abd Ghani,
Ruzheinikov Sergey N.,
Sedelnikova Svetlana E.,
Mohamed Rahmah,
Nathan Sheila,
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/s1744309112004800
Subject(s) - ribosomal protein , cloning (programming) , burkholderia pseudomallei , crystallization , escherichia coli , resolution (logic) , strain (injury) , microbiology and biotechnology , chemistry , ribosomal rna , gene , biology , bacteria , crystallography , ribosome , biochemistry , genetics , rna , organic chemistry , anatomy , artificial intelligence , computer science , programming language
The gene encoding the L1 ribosomal protein from Burkholderia pseudomallei strain D286 has been cloned into the pETBLUE‐1 vector system, overexpressed in Escherichia coli and purified. Crystals of the native protein were grown by the hanging‐drop vapour‐diffusion technique using PEG 3350 as a precipitant and diffracted to beyond 1.65 Å resolution. The crystals belonged to space group P 2 1 2 1 2, with unit‐cell parameters a = 53.6, b = 127.1, c = 31.8 Å and with a single molecule in the asymmetric unit.