Protein expression, crystallization and preliminary X-ray crystallographic studies of YjbK from Bacillus subtilis.
B. subtilis YjbK is a protein with 190 residues of uncharacterized function, it has been annotated by Pfam database as a member of adenylate cyclase family (EC: 4.6.1.1). In order to identify its exact function via structural studies, yjbK gene was amplified from B. subtilis genomic DNA and cloned into expression vector pET21-DEST. The protein was expressed in a soluble form in E. coli and purified to homogeneity. YjbK was crystallized and diffracted to a resolution of 2.0 A in-house. The crystals belong to P1 space group, with unit cell parameters a = 32.38 A, b = 34.69 A, c = 46.02 A, alpha = 96.560 degrees, beta = 99.683 degrees, gamma = 111.333 degrees. There is one molecule per asymmetric unit.
Dai
Xue-Yu
XY
National Laboratory of Protein Engineering and Plant Genetic Engineering, China.
Liu
Yuan
Y
Liang
Yu-He
YH
Zheng
Xiaofeng
X
Luo
Ming
M
Li
Lanfen
L
Su
Xiao-Dong
XD
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D015870:Gene Expression / Q000235:genetics*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins