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Characterization, crystallization and preliminary X-ray analysis of the adhesive domain of SdrE from Staphylococcus aureus.

ABSTRACT: The adhesive domain of SdrE from Staphylococcus aureus was recombinantly expressed in Escherichia coli. The purified protein was identified by SDS-PAGE and MALDI-TOF MS. The protein was crystallized using the vapour-diffusion method in hanging-drop mode with PEG 8000 as the primary precipitating agent. X-ray diffraction data were collected to 1.8 A resolution from a single crystal of the protein. Preliminary X-ray analysis indicated that the crystal belonged to space group P1, with unit-cell parameters a = 40.714, b = 66.355, c = 80.827 A, alpha = 111.19, beta = 93.99, gamma = 104.39 degrees.

SUBMITTER: Xiang H

PROVIDER: S-EPMC2898480 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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Characterization, crystallization and preliminary X-ray analysis of the adhesive domain of SdrE from Staphylococcus aureus.

Xiang Hua H Gao Fangfang F Wang Dacheng D Liu Jing J Hu Jia J Zhang Liqing L Li Shentao S Deng Xuming X

Acta crystallographica. Section F, Structural biology and crystallization communications 20100624 Pt 7

The adhesive domain of SdrE from Staphylococcus aureus was recombinantly expressed in Escherichia coli. The purified protein was identified by SDS-PAGE and MALDI-TOF MS. The protein was crystallized using the vapour-diffusion method in hanging-drop mode with PEG 8000 as the primary precipitating agent. X-ray diffraction data were collected to 1.8 A resolution from a single crystal of the protein. Preliminary X-ray analysis indicated that the crystal belonged to space group P1, with unit-cell par ...[more]

PMID: 20606292

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