The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 å resolution: structural characterization of proline-substitution sites for protein thermostabilization
- 1 May 1997
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 269 (1), 142-153
- https://doi.org/10.1006/jmbi.1997.1018
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Stability and structural analysis of α‐amylase from the antarctic psychrophile Alteromonas haloplanctis A23European Journal of Biochemistry, 1994
- Design of helix endsInternational Journal of Peptide and Protein Research, 1993
- Stabilization of Bacillus stearothermophilus neutral protease by introduction of prolinesFEBS Letters, 1993
- Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with x-ray structure analysis of proline mutantsBiochemistry, 1992
- The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallographyJournal of Applied Crystallography, 1989
- Crystallographic R Factor Refinement by Molecular DynamicsScience, 1987
- Solvent-Accessible Surfaces of Proteins and Nucleic AcidsScience, 1983
- Amino acid distribution in protein secondary structuresInternational Journal of Peptide and Protein Research, 1982
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975