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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*
- 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