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Cloning, overproduction, purification, crystallization and preliminary X-ray diffraction analysis of yeast glutaredoxin Grx5.

ABSTRACT: Grx5 from the yeast Saccharomyces cerevisiae is a monothiol glutaredoxin that is involved in iron-sulfur cluster biogenesis. Here, yeast Grx5 was cloned and overproduced in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Diffraction data for Grx5 were collected to 1.67 A resolution. The crystal of Grx5 belonged to space group R3, with unit-cell parameters a = b = 85.12, c = 48.95 A, alpha = beta = 90.00, gamma = 120.00 degrees .

SUBMITTER: Wang Y

PROVIDER: S-EPMC2688435 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Cloning, overproduction, purification, crystallization and preliminary X-ray diffraction analysis of yeast glutaredoxin Grx5.

Wang Yi Y He Yong Xing YX Yu Jiang J Zhou Cong Zhao CZ

Acta crystallographica. Section F, Structural biology and crystallization communications 20090523 Pt 6

Grx5 from the yeast Saccharomyces cerevisiae is a monothiol glutaredoxin that is involved in iron-sulfur cluster biogenesis. Here, yeast Grx5 was cloned and overproduced in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Diffraction data for Grx5 were collected to 1.67 A resolution. The crystal of Grx5 belonged to space group R3, with unit-cell parameters a = b = 85.12, c = 48.95 A, alpha = beta = 90.00, gamma = 120.00 degrees . ...[more]

PMID: 19478456

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