Crystallization and preliminary X-ray diffraction study of the bacterially expressed Fv from the monoclonal anti-lysozyme antibody D1.3 and of its complex with the antigen, lysozyme

J Mol Biol. 1990 Jun 20;213(4):617-9. doi: 10.1016/S0022-2836(05)80248-7.

Abstract

The associated heavy (VH) and light (VL) chain variable domains (Fv) of the monoclonal anti-lysozyme antibody D1.3, secreted from Escherichia coli, have been crystallized in their antigen-bound and free forms. FvD1.3 gives tetragonal crystals, space group P4(1)2(1)2 (or P4(3)2(1)2), with a = 90.6 A, c = 56.4 A. The FvD1.3-lysozyme complex crystallizes in space group C2, with a = 129.2 A, b = 60.8 A, c = 56.9 A and beta = 119.3 degrees. The crystals contain one molecule of Fv or of the Fv-lysozyme complex in their asymmetric units and diffract X-rays to high resolution, making them suitable for X-ray crystallographic studies.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal / genetics*
  • Base Sequence
  • Crystallization
  • Escherichia coli / genetics
  • Escherichia coli / immunology*
  • Immunoglobulin Heavy Chains* / genetics
  • Immunoglobulin Heavy Chains* / immunology
  • Immunoglobulin Light Chains* / genetics
  • Immunoglobulin Light Chains* / immunology
  • Immunoglobulin Variable Region* / genetics
  • Immunoglobulin Variable Region* / immunology
  • Molecular Sequence Data
  • Muramidase / immunology*
  • X-Ray Diffraction

Substances

  • Antibodies, Monoclonal
  • Immunoglobulin Heavy Chains
  • Immunoglobulin Light Chains
  • Immunoglobulin Variable Region
  • Muramidase