Structure and refinement of penicillopepsin at 1.8 Å resolution
- 1 January 1983
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 163 (2), 299-361
- https://doi.org/10.1016/0022-2836(83)90008-6
Abstract
No abstract availableThis publication has 55 references indexed in Scilit:
- Protein structure refinement: Streptomyces griseus serine protease A at 1.8 Å resolutionJournal of Molecular Biology, 1979
- Structure of acid protease from Endothia parasitica in crosslinked form at 2.45-.ANG. resolutionBiochemistry, 1979
- Structure of erythrocruorin in different ligand states refined at 1·4 Å resolutionJournal of Molecular Biology, 1979
- Conformation of amino acid side-chains in proteinsJournal of Molecular Biology, 1978
- Experience with fast Fourier least squares in the refinement of the crystal structure of rhombohedral 2-zinc insulin at 1.5 Å resolutionActa Crystallographica Section A, 1978
- Radiation damage in protein crystallographyJournal of Molecular Biology, 1976
- Activation of the action of penicillopepsin on leucyl-tyrosyl-amide by a non-substrate peptide and evidence for a conformational change associated with a secondary binding siteBiochemical and Biophysical Research Communications, 1974
- Environment and exposure to solvent of protein atoms. Lysozyme and insulinJournal of Molecular Biology, 1973
- Conformation of twisted β-pleated sheets in proteinsJournal of Molecular Biology, 1973
- Refinement of bond angles of an α-helixJournal of Molecular Biology, 1967