Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris.
Xanthomonas campestris pv. campestris is the causative agent of black rot, one of the major worldwide diseases of cruciferous crops. Its genome encodes approximately 4500 proteins, roughly one third of which have unknown function. XC2382 is one such protein, with a MW of 14.2 kDa. Based on a bioinformatics study, it was annotated as an ApaG gene product that serves multiple functions. The ApaG protein has been overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of at least 2.30 A. They are tetragonal and belong to space group P4(1/3), with unit-cell parameters a = b = 57.6, c = 122.9 A. There are two, three or four molecules in the asymmetric unit.
Chin
Ko-Hsin
KH
Institute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan.
Chou
Chia-Cheng
CC
Lee
Cheng-Chung
CC
Shr
Hui-Lin
HL
Lyu
Ping-Chiang
PC
Wang
Andrew H-J
AH
Chou
Shan-Ho
SH
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D019295:Computational Biology; D015925:Cryopreservation; D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D016680:Genome, Bacterial; D009991:Oscillometry; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D016959:Xanthomonas campestris / Q000378:metabolism*
D001426:Bacterial Proteins; D011994:Recombinant Proteins