PMID:22139174
| Citation |
Qiu, X, Yuan, Y and Gao, Y (2011) Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67:1590-4 |
|---|---|
| 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°. |
| Links |
PubMed PMC3232147 Online version:10.1107/S1744309111039960 |
| Keywords |
Amino Acid Sequence; Animals; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Gene Expression; Humans; Molecular Sequence Data; Phosphoribosylaminoimidazolecarboxamide Formyltransferase/chemistry; Phosphoribosylaminoimidazolecarboxamide Formyltransferase/genetics; Phosphoribosylaminoimidazolecarboxamide Formyltransferase/isolation & purification; Sequence Alignment |
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