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Expression, crystallization and preliminary X-ray studies of the immunoglobulin-like domain 3 of human palladin.

ABSTRACT: Palladin is a member of the recently discovered palladin/myotilin/myopalladin family, the members of which associate with alpha-actinin. Palladin may play important roles in actin stress-fibre formation, cell adhesion and migration. The immunoglobulin-like domain 3 of human palladin has been overexpressed in Escherichia coli and crystallized suitable for X-ray crystallographic study. Crystals have been obtained using the vapour-diffusion method and belong to space group P2(1). X-ray diffraction data were collected in-house to 1.8 A resolution from a single crystal. The unit-cell parameters are a = 40.9, b = 33.3, c = 34.8 A, beta = 90.3 degrees . One molecule was predicted to be present in the asymmetric unit.

SUBMITTER: Liang W

PROVIDER: S-EPMC2243106 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature

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Expression, crystallization and preliminary X-ray studies of the immunoglobulin-like domain 3 of human palladin.

Liang Wenxue W Yang Haitao H Xue Xiaoyu X Huang Qiuhua Q Bartlam Mark M Chen Saijuan S

Acta crystallographica. Section F, Structural biology and crystallization communications 20060531 Pt 6

Palladin is a member of the recently discovered palladin/myotilin/myopalladin family, the members of which associate with alpha-actinin. Palladin may play important roles in actin stress-fibre formation, cell adhesion and migration. The immunoglobulin-like domain 3 of human palladin has been overexpressed in Escherichia coli and crystallized suitable for X-ray crystallographic study. Crystals have been obtained using the vapour-diffusion method and belong to space group P2(1). X-ray diffraction ...[more]

PMID: 16754980

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