Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes

Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):187-8. doi: 10.1107/s090744499901495x.

Abstract

The 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes has been expressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals were grown using a salting-in technique. Crystals have a tetragonal plate shape and belong to the C2 space group, with unit-cell parameters a = 163.9, b = 106.5, c = 93.5 A, beta = 95.5 degrees. The crystals diffract to 2.8 A resolution.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Cytoskeletal Proteins*
  • Erythrocyte Membrane / chemistry*
  • Humans
  • Membrane Proteins / blood*
  • Membrane Proteins / chemistry*
  • Molecular Weight
  • Neuropeptides*
  • Protein Binding
  • Protein Structure, Tertiary

Substances

  • Cytoskeletal Proteins
  • Membrane Proteins
  • Neuropeptides
  • erythrocyte membrane band 4.1 protein
  • erythrocyte membrane protein band 4.1-like 1