Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of YvoA from Bacillus subtilis
Author(s) -
Resch Marcus,
Roth Heide Marie,
Kottmair Mathias,
Sevvana Madhumati,
Bertram Ralph,
Titgemeyer Fritz,
Muller Yves A.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109008628
Subject(s) - bacillus subtilis , escherichia coli , cloning (programming) , resolution (logic) , affinity chromatography , monoclinic crystal system , crystallization , chemistry , size exclusion chromatography , recombinant dna , crystallography , chromatography , biology , microbiology and biotechnology , bacteria , biochemistry , crystal structure , genetics , gene , organic chemistry , enzyme , artificial intelligence , computer science , programming language
The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli . The protein was purified by immobilized metal‐affinity chromatography and size‐exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 Å resolution. The crystals belonged to the monoclinic space group C 2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.