Back to Search
Start Over
Crystal parameters and molecular replacement of an anticholera toxin peptide complex.
- Source :
-
Proteins [Proteins] 1991; Vol. 11 (3), pp. 218-22. - Publication Year :
- 1991
-
Abstract
- TE33 is an Fab fragment of a monoclonal antibody raised against a 15-residue long peptide (CTP3), corresponding in sequence to residues 50-64 of the cholera toxin B subunit. Crystals of the complex between TE33 and CTP3 have been grown from 20% (w/v) polyethylene glycol-8000 at pH 4.0. The crystals are orthorhombic, space group P2(1)2(1)2, with unit cell dimensions a = 104.15, b = 110.61, and c = 40.68 A. X-Ray data have been collected to a resolution of 2.3 A. The asymmetric unit contains one molecule of Fab and one molecule of CTP3. The presence of CTP3 has been demonstrated by fluorescence quenching of the dissolved crystal after X-ray data collection. A molecular replacement solution was found based on the coordinates of DB3, an antiprogesterone Fab fragment.
- Subjects :
- Antibodies, Monoclonal
Binding Sites, Antibody
Cholera Toxin immunology
Crystallization
Crystallography
Immunoglobulin Fab Fragments immunology
Peptide Fragments immunology
Protein Conformation
Sequence Homology, Nucleic Acid
Software
Cholera Toxin chemistry
Immunoglobulin Fab Fragments chemistry
Peptide Fragments chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0887-3585
- Volume :
- 11
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 1749774
- Full Text :
- https://doi.org/10.1002/prot.340110306