TY - JOUR
T1 - Expression, purification, crystallization and preliminary X-ray analysis of a DNA-binding protein from Methanococcus jannaschii
AU - Wang, Ganggang
AU - Guo, Rong
AU - Bartlam, Mark
AU - Xue, Hong
AU - Yang, Haitao
AU - Liu, Yiwei
AU - Huang, Li
AU - Rao, Zihe
PY - 2002
Y1 - 2002
N2 - 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 P6122/P6522, with unit-cell parameters a = b = 50.85, c = 124.02 Å, α = β = 90, γ = 120°. The crystals diffracted to a maximum resolution of 2.2 Å at 100 K using Cu Kα radiation. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (VM) of 2.4 Å3 Da-1 and a solvent content of 49% by volume. A full set of X-ray diffraction data was collected to 2.2 Å from the native crystal.
AB - 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 P6122/P6522, with unit-cell parameters a = b = 50.85, c = 124.02 Å, α = β = 90, γ = 120°. The crystals diffracted to a maximum resolution of 2.2 Å at 100 K using Cu Kα radiation. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (VM) of 2.4 Å3 Da-1 and a solvent content of 49% by volume. A full set of X-ray diffraction data was collected to 2.2 Å from the native crystal.
UR - https://www.webofscience.com/wos/woscc/full-record/WOS:000176342000031
UR - https://www.scopus.com/pages/publications/0035997159
U2 - 10.1107/S0907444902007679
DO - 10.1107/S0907444902007679
M3 - Journal Article
C2 - 12077456
SN - 0907-4449
VL - 58
SP - 1240
EP - 1242
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 7
ER -