Crystallization and preliminary crystallographic analysis of the N-terminal two domain fragment of vascular cell adhesion molecule-1 (VCAM-1)

Proteins. 1994 Nov;20(3):287-90. doi: 10.1002/prot.340200310.

Abstract

A molecular fragment comprising the first two domains of the human vascular cell adhesion molecule-1 (VCAM-1) has been crystallized by the vapor diffusion method. Two crystal forms have been examined by X-ray analysis: One crystal form belongs to the space group C2 with two molecules in the asymmetric unit and cell parameters: a = 122.1 A, b = 48.9 A, c = 73.4 A, and beta = 117.4 degrees. The other crystal form belongs to the space group P2(1) with one molecule in the asymmetric unit and cell parameters: a = 40.4 A, b = 45.7 A, c = 54.7 A, and beta = 100.5 degrees. Diffraction data up to 1.9 A resolution have been collected for the C2 crystal form.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • Cell Adhesion Molecules / chemistry*
  • Cricetinae
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Protein Conformation
  • Vascular Cell Adhesion Molecule-1

Substances

  • Cell Adhesion Molecules
  • Peptide Fragments
  • Vascular Cell Adhesion Molecule-1