Expression, purification, crystallization and preliminary X-ray analysis of a DNA-binding protein from Methanococcus jannaschii.
A small DNA-binding protein of 87 amino-acid residues from the hyperthermophilic archaeon Methanococcus jannaschii (Mja10b) was cloned and overexpressed in Escherichia coli. The protein was crystallized and the crystals belong to the space group P6(1)22/P6(5)22, with unit-cell parameters a = b = 50.85, c = 124.02 A, alpha = beta = 90, gamma = 120 degrees. The crystals diffracted to a maximum resolution of 2.2 A at 100 K using Cu Kalpha radiation. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (V(M)) of 2.4 A(3) Da(-1) and a solvent content of 49% by volume. A full set of X-ray diffraction data was collected to 2.2 A from the native crystal.
Wang
Ganggang
G
MOE Laboratory of Protein Science and Laboratory of Structural Biology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
Guo
Rong
R
Bartlam
Mark
M
Xue
Hong
H
Yang
Haitao
H
Liu
Yiwei
Y
Huang
Li
L
Rao
Zihe
Z
D018360:Crystallography, X-Ray / Q000379:methods*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D017017:Methanococcus / Q000737:chemistry*; D010957:Plasmids / Q000378:metabolism
D004268:DNA-Binding Proteins