Open AccessExpression, crystallization and preliminary X‐ray studies of the immunoglobulin‐like domain 3 of human palladin
Author(s) -
Liang Wenxue,
Yang Haitao,
Xue Xiaoyu,
Huang Qiuhua,
Bartlam Mark,
Chen Saijuan
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106016411
Subject(s) - crystallization , immunoglobulin superfamily , crystallography , adhesion , antibody , immunoglobulin domain , materials science , cell , chemistry , biology , biochemistry , immunology , organic chemistry , composite material
Palladin is a member of the recently discovered palladin/myotilin/myopalladin family, the members of which associate with α‐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 P 2 1 . X‐ray diffraction data were collected in‐house to 1.8 Å resolution from a single crystal. The unit‐cell parameters are a = 40.9, b = 33.3, c = 34.8 Å, β = 90.3°. One molecule was predicted to be present in the asymmetric unit.