Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 A resolution.
Open Access
- 4 January 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (2) , 585-597
- https://doi.org/10.1016/s0021-9258(17)38249-2
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Similarity of three-dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunitJournal of Molecular Biology, 1976
- Specific interaction between VH and VL regions of human monoclonal immunoglobulinsJournal of Molecular Biology, 1976
- Different degrees of interspecies homology in immunoglobulin λ chain constant domain correlated with three-dimensional structureNature, 1975
- Crystal and Molecular Structure of a Dimer Composed of the Variable Portions of the Bence-Jones Protein REIEuropean Journal of Biochemistry, 1974
- Amino acid sequence of the λ light chain of a human myeloma immunoglobulin (IgG new)Biochemistry, 1974
- Real-space refinement of the structure of hen egg-white lysozymeJournal of Molecular Biology, 1974
- Comparison of super-secondary structures in proteinsJournal of Molecular Biology, 1973
- Variability in the Lambda Light Chain Sequences of Mouse AntibodyNature, 1970
- The matching of physical models to three-dimensional electron-density maps: A simple optical deviceJournal of Molecular Biology, 1968
- Crystallization of Fragment Fab of human IgG myeloma proteinsBiochemical and Biophysical Research Communications, 1968