Open AccessCloning, purification and crystallographic analysis of a hypothetical protein, BPSL1549, from Burkholderia pseudomallei
Author(s) -
CruzMigoni Abimael,
Ruzheinikov Sergey N.,
Sedelnikova Svetlana E.,
Obeng Barbara,
Chieng Sylvia,
Mohamed Rahmah,
Nathan Sheila,
Baker Patrick J.,
Rice David W.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111028995
Subject(s) - burkholderia pseudomallei , cloning (programming) , escherichia coli , burkholderia , synchrotron radiation , resolution (logic) , crystallography , chemistry , microbiology and biotechnology , bacteria , biology , physics , biochemistry , gene , genetics , optics , artificial intelligence , computer science , programming language
Burkholderia pseudomallei BPSL1549, a putative protein of unknown function, has been overexpressed in Escherichia coli , purified and subsequently crystallized by the hanging‐drop vapour‐diffusion method using PEG as a precipitant to give crystals with overall dimensions of 0.15 × 0.15 × 0.1 mm. Native data were collected to 1.47 Å resolution at the European Synchrotron Radiation Facility (ESRF). The crystals belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 37.1, b = 45.4, c = 111.9 Å and with a single polypeptide chain in the asymmetric unit.