Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 Å resolution
- 2 May 1997
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 268 (2), 449-459
- https://doi.org/10.1006/jmbi.1997.0968
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Role of N-linked glycosylation of lecithin: cholesterol acyltransferase in lipoprotein substrate specificityBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Differences in the thermostabilities of barley (1→3,1→4)-β-glucanases are only partly determined byN-glycosylationFEBS Letters, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- A kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor mieheiBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8A˚resolutionJournal of Molecular Biology, 1990
- Protein chemical characterization of Mucor pusillus aspartic proteinase Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachmentFEBS Letters, 1988
- Functional characterization of Asp‐317 mutant of human renin expressed in COS cellsFEBS Letters, 1988
- Repeated seeding technique for growing large single crystals of proteinsJournal of Molecular Biology, 1981