X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution
- 1 November 1986
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 192 (1) , 133-154
- https://doi.org/10.1016/0022-2836(86)90470-5
Abstract
No abstract availableThis publication has 50 references indexed in Scilit:
- Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinusJournal of Molecular Biology, 1985
- Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozymeJournal of Molecular Biology, 1985
- Hemoglobin tertiary structural change on ligand binding its role in the co-operative mechanismJournal of Molecular Biology, 1983
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Crystallographic refinement of rubredoxin at 1·2 Å resolutionJournal of Molecular Biology, 1980
- Structure of erythrocruorin in different ligand states refined at 1·4 Å resolutionJournal of Molecular Biology, 1979
- Stereochemistry of carbon monoxide binding to myoglobin and hemoglobinJournal of Molecular Biology, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977