Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level
- 1 December 1998
- Vol. 6 (12) , 1503-1516
- https://doi.org/10.1016/s0969-2126(98)00149-x
Abstract
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This publication has 51 references indexed in Scilit:
- The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 å resolution: structural characterization of proline-substitution sites for protein thermostabilizationJournal of Molecular Biology, 1997
- The structure of human pancreaticα-amylase at 1.8 Å resolution and comparisons with related enzymesProtein Science, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Protein Hydration Observed by X-ray DiffractionJournal of Molecular Biology, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Refined Molecular Structure of Pig Pancreatic α-Amylase at 2·1 Å ResolutionJournal of Molecular Biology, 1994
- Starch- and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymesProtein Journal, 1993
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Aromatic-Aromatic Interaction: A Mechanism of Protein Structure StabilizationScience, 1985
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983