Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human

Chao-Neng Ji; Gang Ying; Ying-Feng Deng; Shu Chen; Wen-Hong Zhang; Guang Shu; Yi Xie; Yu-Min Mao

doi:10.1107/s0907444903008588

Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1109-10. doi: 10.1107/s0907444903008588. Epub 2003 May 23.

Authors

Chao-Neng Ji¹, Gang Ying, Ying-Feng Deng, Shu Chen, Wen-Hong Zhang, Guang Shu, Yi Xie, Yu-Min Mao

Affiliation

¹ State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.

PMID: 12777790
DOI: 10.1107/s0907444903008588

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).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Escherichia coli
GMP Reductase
Humans
Isoenzymes / chemistry
Isoenzymes / isolation & purification
Molecular Sequence Data
NADH, NADPH Oxidoreductases / chemistry*
NADH, NADPH Oxidoreductases / isolation & purification
Reverse Transcriptase Polymerase Chain Reaction
X-Ray Diffraction

Substances

Isoenzymes
NADH, NADPH Oxidoreductases
GMP Reductase

Associated data

GENBANK/AF419346
PDB/1EEP