Published in

International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(64), p. 692-696, 2008

DOI: 10.1107/s1744309108018307

Links

Tools

Export citation

Search in Google Scholar

Expression, purification and preliminary X-ray diffraction studies of the transcriptional factor PyrR fromBacillus halodurans

Journal article published in 2008 by Rodrigo Arreola ORCID, Anita Vega-Miranda, Armando Gómez-Puyou, Ruy Pérez-Montfort, Enrique Merino-Pérez, Alfredo Torres-Larios ORCID
This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Green circle
Postprint: archiving allowed
Upload
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

Abstract

The PyrR transcriptional regulator is widely distributed in bacteria. This RNA-binding protein is involved in the control of genes involved in pyrimidine biosynthesis, in which uridyl and guanyl nucleotides function as effectors. Here, the crystallization and preliminary X-ray diffraction analysis of two crystal forms of Bacillus halodurans PyrR are reported. One of the forms belongs to the monoclinic space group P2(1) with unit-cell parameters a = 59.7, b = 87.4, c = 72.1 A, beta = 104.4 degrees , while the other form belongs to the orthorhombic space group P22(1)2(1) with unit-cell parameters a = 72.7, b = 95.9, c = 177.1 A. Preliminary X-ray diffraction data analysis and molecular-replacement solution revealed the presence of four and six monomers per asymmetric unit; a crystallographic tetramer is formed in both forms.