title: Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human.
abstract: 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).
authors.affiliation: State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.
authors.forename: Chao-Neng
authors.initials: CN
authors.lastname: Ji
authors.forename: Gang
authors.initials: G
authors.lastname: Ying
authors.forename: Ying-Feng
authors.initials: YF
authors.lastname: Deng
authors.forename: Shu
authors.initials: S
authors.lastname: Chen
authors.forename: Wen-Hong
authors.initials: WH
authors.lastname: Zhang
authors.forename: Guang
authors.initials: G
authors.lastname: Shu
authors.forename: Yi
authors.initials: Y
authors.lastname: Xie
authors.forename: Yu-Min
authors.initials: YM
authors.lastname: Mao
mesh_terms: 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
chemical_list: D007527:Isoenzymes; D009247:NADH, NADPH Oxidoreductases; D050899:GMP Reductase