Hyperthermostable Protein Structure Maintained by Intra and Inter-helix Ion-pairs in Archaeal O6-Methylguanine-DNA Methyltransferase
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (3), 707-716
- https://doi.org/10.1006/jmbi.1999.3100
Abstract
No abstract availableKeywords
Funding Information
- University of Tsukuba
- Life Science Center for Survival Dynamics Tsukuba Advanced Research Alliance
- Japan Society for the Promotion of Science
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 41 references indexed in Scilit:
- Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin OxidoreductaseScience, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Kinetic and DNA-Binding Properties of Recombinant Human O6-Methylguanine-DNA MethyltransferaseArchives of Biochemistry and Biophysics, 1993
- ALSCRIPT: a tool to format multiple sequence alignmentsProtein Engineering, Design and Selection, 1993
- X‐ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosusProtein Science, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Slow-cooling protocols for crystallographic refinement by simulated annealingActa Crystallographica Section A Foundations of Crystallography, 1990
- Crystallographic R Factor Refinement by Molecular DynamicsScience, 1987
- Ion-pairs in proteinsJournal of Molecular Biology, 1983
- Genetic studies of the lac repressorJournal of Molecular Biology, 1977