Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.
Open Access
- 1 February 1991
- journal article
- abstracts
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 266 (5), 2864-2871
- https://doi.org/10.1016/s0021-9258(18)49927-9
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Crystal structure of neutral protease from Bacillus cereus refined at 3.0A˚resolution and comparison with the homologous but more thermostable enzyme thermolysinJournal of Molecular Biology, 1988
- An efficient general-purpose least-squares refinement program for macromolecular structuresActa Crystallographica Section A Foundations of Crystallography, 1987
- Protein, DNA, and Virus Crystallography with a Focused Imaging Proportional CounterScience, 1986
- The Primary Structure ofBacillus cereusNeutral Proteinase and Comparison with Thermolysin andBacillus subtilisNeutral ProteinaseBiological Chemistry Hoppe-Seyler, 1986
- Structure of thermolysin refined at 1.6 Å resolutionJournal of Molecular Biology, 1982
- A limited-range step-scan method for collecting X-ray diffraction dataActa Crystallographica Section A, 1979
- An explanation for the rare occurrence of cis peptide units in proteins and polypeptidesJournal of Molecular Biology, 1976
- The refinement of the heavy-atom parameters in the presence of non-crystallographic symmetryActa Crystallographica Section A, 1976
- Barrier to internal rotation in amides. IV. N,N-Dimethylamides. Substituent and solvent effectsThe Journal of Physical Chemistry, 1972
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967