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Preliminary Crystallographic Data and Primary Sequence for Anti-peptide Fab' B13I2 and Its Complex with the C-helix Peptide from Myohemerythrin*

Authors :
Stura, E A
Stanfield, R L
Fieser, T M
Balderas, R S
Smith, L R
Lerner, R A
Wilson, I A
Source :
Journal of Biological Chemistry; September 1989, Vol. 264 Issue: 26 p15721-15725, 5p
Publication Year :
1989

Abstract

Crystals of the Fab' fragment from the monoclonal anti-peptide antibody B13I2 and of the Fab'-peptide antigen complex have been characterized. The monoclonal antibodies were raised against a synthetic homologue of the C-helix of myohemerythrin (residues 69–87 in myohemerythrin). The Fab'-peptide complex crystallizes in space group P6322 with unit cell dimensions a= b= 142.5 Å, c= 101.5 Å, α = β = 90°, γ = 120°, and Z= 1. The native Fab' crystallizes in space group P212121with unit cell dimensions a= 98.0 Å, b= 151.7 Å, c= 80.8 Å,α = β = γ = 90°, and Z= 2. Both crystal forms diffract to beyond 2.6 Å resolution. We also report the cDNA and predicted amino acid sequences for the variable regions of both the light and heavy chains of this anti-peptide antibody.

Details

Language :
English
ISSN :
00219258 and 1083351X
Volume :
264
Issue :
26
Database :
Supplemental Index
Journal :
Journal of Biological Chemistry
Publication Type :
Periodical
Accession number :
ejs55933315
Full Text :
https://doi.org/10.1016/S0021-9258(19)84892-5