title: Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli.
abstract: In bacteria and eukaryotes, the last two steps of de novo purine biosynthesis are catalyzed by bifunctional purine-biosynthesis protein (PurH), which is composed of two functionally independent domains linked by a flexible region. The N-terminal domain possesses IMP cyclohydrolase activity and the C-terminal domain possesses aminoimidazole-4-carboxamide ribonucleotide transformylase activity. This study reports the expression, purification, crystallization and preliminary X-ray crystallographic analysis of PurH from Escherichia coli with an N-terminal His(6) tag. The crystals diffracted to a maximum resolution of 3.05 Å and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 76.37, b = 132.15, c = 82.64 Å, β = 111.86°.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
authors.forename: Xiaoting
authors.initials: X
authors.lastname: Qiu
authors.forename: Ye
authors.initials: Y
authors.lastname: Yuan
authors.forename: Yongxiang
authors.initials: Y
authors.lastname: Gao
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D015870:Gene Expression; D006801:Humans; D008969:Molecular Sequence Data; D051027:Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D016415:Sequence Alignment
chemical_list: D051027:Phosphoribosylaminoimidazolecarboxamide Formyltransferase