Crystallization of a DNA and N-acetylserine binding fragment (residues 1 to 233) of Klebsiella aerogenes CysB protein, a member of the LysR family.
CysB protein is a positive regulator of transcription of genes involved in cysteine biosynthesis in bacteria and a member of the LysR family of DNA binding proteins. A 233-residue N-terminal chymotryptic fragment of the protein, with DNA and N-acetylserine binding activity, has been crystallized in the presence of monomethyl-polyethylene glycol 750. The crystals diffract to 2.5 A (1 A = 0.1 nm) spacing on a rotating copper anode X-ray source and to 2.1 A spacing using synchrotron radiation and are suitable for structural studies. The space group is P2(1)2(1)2 with unit cell dimensions of a = 68.8 A, b = 109.9 A and c = 33.5 A. On the assumption that the asymmetric unit comprises one monomer, the crystals have a solvent content of approximately 50%.
Tyrrell
R
R
Department of Chemistry, University of York.
Davies
G J
GJ
Wilson
K S
KS
Wilkinson
A J
AJ
D001426:Bacterial Proteins / Q000737:chemistry / Q000648:ultrastructure*; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000648:ultrastructure*; D018257:Helix-Loop-Helix Motifs; D007711:Klebsiella pneumoniae / Q000737:chemistry*; D010446:Peptide Fragments; D011485:Protein Binding; D012694:Serine / Q000031:analogs & derivatives / Q000378:metabolism; D014157:Transcription Factors / Q000648:ultrastructure
D001426:Bacterial Proteins; C062886:CysB protein, Bacteria; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D014157:Transcription Factors; D012694:Serine; D003545:Cysteine; C012162:N-acetylserine