Expression, crystallization and preliminary X-ray studies of the immunoglobulin-like domain 3 of human palladin.
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.
Liang
Wenxue
W
State Key Laboratory of Medical Genomics and Shanghai Institute of Hematology, Rui Jin Hospital Affiliated to Shanghai Second Medical University, Shanghai 200025, People's Republic of China.
Yang
Haitao
H
Xue
Xiaoyu
X
Huang
Qiuhua
Q
Bartlam
Mark
M
Chen
Saijuan
S
D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D010750:Phosphoproteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D012997:Solvents; D014961:X-Ray Diffraction
D003598:Cytoskeletal Proteins; C412722:PALLD protein, human; D010750:Phosphoproteins; D012997:Solvents