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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, ? = 111.86°.

SUBMITTER: Qiu X

PROVIDER: S-EPMC3232147 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli.

Qiu Xiaoting X Yuan Ye Y Gao Yongxiang Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20111126 Pt 12

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 ...[more]

PMID: 22139174

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