Crystal parameters and molecular replacement of an anticholera toxin peptide complex.
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.
Shoham
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Department of Biochemistry, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106.
Proctor
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Hughes
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Baldwin
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ET
D000911:Antibodies, Monoclonal; D001666:Binding Sites, Antibody; D002772:Cholera Toxin / Q000737:chemistry* / Q000276:immunology; D003460:Crystallization; D003461:Crystallography; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry* / Q000276:immunology; D010446:Peptide Fragments / Q000737:chemistry* / Q000276:immunology; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012984:Software
D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D010446:Peptide Fragments; C050310:cholera toxin, B subunit (50-64); D002772:Cholera Toxin