Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human.
GMP reductase 2 from human has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 110.6, c = 209.8 A, alpha = beta = 90, gamma = 120 degrees. Diffraction data were collected to 3.0 A with a completeness of 100% (100% for the last shell), an R(merge) value of 0.089 (0.189) and an I/sigma(I) value of 7.3 (3.2).
Ji
Chao-Neng
CN
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.
Ying
Gang
G
Deng
Ying-Feng
YF
Chen
Shu
S
Zhang
Wen-Hong
WH
Shu
Guang
G
Xie
Yi
Y
Mao
Yu-Min
YM
D003460:Crystallization; D004926:Escherichia coli; D050899:GMP Reductase; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D020133:Reverse Transcriptase Polymerase Chain Reaction; D014961:X-Ray Diffraction
D007527:Isoenzymes; D009247:NADH, NADPH Oxidoreductases; D050899:GMP Reductase