Crystal structure of an anti-Lewis a Fab determined by molecular replacement methods
- 20 November 1987
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 198 (2) , 351-355
- https://doi.org/10.1016/0022-2836(87)90318-4
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Three-dimensional structure of a complex of antibody with influenza virus neuraminidaseNature, 1987
- Antibody Fab assembly: The interface residues between CH1 and CLMolecular Immunology, 1986
- Three-Dimensional Structure of an Antigen-Antibody Complex at 2.8 Å ResolutionScience, 1986
- Phosphocholine binding immunoglobulin Fab McPC603Journal of Molecular Biology, 1986
- The galactan‐binding immunoglobulin Fab J539: An x‐ray diffraction study at 2.6‐Å resolutionProteins-Structure Function and Bioinformatics, 1986
- A MWPC X-ray diffractometer facility for protein crystallographyNuclear Instruments and Methods in Physics Research, 1984
- Structural Basis of Antibody FunctionAnnual Review of Immunology, 1983
- Calmodulin, S-100, and crayfish sarcoplasmic calcium-binding protein crystals suitable for X-ray diffraction studies.Journal of Biological Chemistry, 1980
- Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolutionJournal of Molecular Biology, 1980
- Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolutionJournal of Molecular Biology, 1976