title: Protein preparation, crystallization and preliminary crystallographic studies of Bacillus subtilis glycinamide ribonucleotide transformylase.
abstract: Glycinamide ribonucleotide transformylase (GART) catalyzes the transfer of a formyl group from formyl tetrahydrofolate (FTHF) to glycinamide ribonucleotide (GAR), which is an essential step in the de novo synthesis pathway of purines. In Bacillus subtilis, GART is encoded by the gene purN. In order to study the structure and function of B. subtilis GART, the purN gene was amplified, cloned into an expression vector and expressed in soluble form in Escherichia coli. The protein was purified to homogeneity and crystals suitable for X-ray data collection were obtained. These crystals diffracted to 2.5 A resolution and belonged to space group P3(1)21, with unit-cell parameters a = b = 95.5, c = 64.0 A.
authors: The National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
authors: Yu-He
authors: YH
authors: Liang
authors: Xiang-Yu
authors: XY
authors: Liu
authors: Juan
authors: J
authors: Wang
authors: Lan-Fen
authors: LF
authors: Li
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D051026:Phosphoribosylglycinamide Formyltransferase / Q000737:chemistry*; D012996:Solutions
chemical_list: D012996:Solutions; D051026:Phosphoribosylglycinamide Formyltransferase