Format

Send to

Choose Destination
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt 4):410-4. doi: 10.1107/S1744309109008628. Epub 2009 Mar 26.

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis.

Author information

1
Lehrstuhl für Biotechnik, Department of Biology, Friederich-Alexander University Erlangen-Nuremberg, Erlangen, Germany.

Abstract

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 A resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.

PMID:
19342794
PMCID:
PMC2664774
DOI:
10.1107/S1744309109008628
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center