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Crystallization and preliminary X-ray diffraction characterisation of both a native and selenomethionyl VLA-4 binding fragment of VCAM-1.

Authors
  • Bottomley, M J
  • Robinson, R C
  • Driscoll, P C
  • Harlos, K
  • Stuart, D I
  • Aplin, R T
  • Clements, J M
  • Jones, E Y
  • Dudgeon, T J
Type
Published Article
Journal
Journal of molecular biology
Publication Date
Dec 09, 1994
Volume
244
Issue
4
Pages
464–468
Identifiers
PMID: 7527465
Source
Medline
License
Unknown

Abstract

Soluble fragments of the extracellular region of vascular cell adhesion molecule 1 (VCAM-1) expressed in Escherichia coli retain functional adhesive activity. An integrin (VLA-4) binding fragment consisting of the N-terminal two immunoglobulin-like domains (VCAM-d1,2) has been crystallized. The crystals belong to space group P2(1)2(1)2(1) with cell dimensions of a = 52.7 A, b = 66.5 A, c = 113.2 A and contain two molecules in the crystallographic asymmetric unit. A batch of protein produced in the standard E. coli strain (HW1110), but grown in the presence of selenomethionine enriched media, showed 85% incorporation of selenium in place of sulphur at methionine residues. The selenomethionyl VCAM-d1,2 was crystallized by microseeding techniques initially using the native crystals for nucleation. Both native and selenomethionyl crystals diffract X-rays to a minimum Bragg spacing of 1.8 A.

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