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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):556-8. doi: 10.1107/S1744309106016411. Epub 2006 May 31.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization / methods
  • Cytoskeletal Proteins / chemistry*
  • Escherichia coli / genetics
  • Humans
  • Phosphoproteins / chemistry*
  • Protein Structure, Tertiary
  • Solvents
  • X-Ray Diffraction

Substances

  • Cytoskeletal Proteins
  • PALLD protein, human
  • Phosphoproteins
  • Solvents