1. Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli.
- Author
-
Qiu X, Yuan Y, and Gao Y
- Subjects
- Amino Acid Sequence, Animals, Crystallization, Crystallography, X-Ray, Gene Expression, Humans, Molecular Sequence Data, Phosphoribosylaminoimidazolecarboxamide Formyltransferase genetics, Phosphoribosylaminoimidazolecarboxamide Formyltransferase isolation & purification, Sequence Alignment, Escherichia coli enzymology, Phosphoribosylaminoimidazolecarboxamide Formyltransferase chemistry
- 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°.
- Published
- 2011
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