Crystal Structure of a Novel-Type Archaeal Rubisco with Pentagonal Symmetry
- 1 June 2001
- Vol. 9 (6) , 473-481
- https://doi.org/10.1016/s0969-2126(01)00608-6
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
- Core Research for Evolutional Science and Technology
- Japan Society for the Promotion of Science
- Japan Science and Technology Corporation
This publication has 48 references indexed in Scilit:
- The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphateJournal of Molecular Biology, 2000
- Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structureJournal of Molecular Biology, 1999
- The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded β-barrel formed by β-strands from four subunitsJournal of Molecular Biology, 1999
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphateJournal of Molecular Biology, 1997
- Large Structures at High Resolution: The 1.6 Å Crystal Structure of Spinach Ribulose-1,5- Bisphosphate Carboxylase/Oxygenase Complexed with 2-Carboxyarabinitol BisphosphateJournal of Molecular Biology, 1996
- Weissenberg camera for macromolecules with imaging plate data collection system at the Photon Factory: Present status and future plan (invited)Review of Scientific Instruments, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2·4 Å resolutionJournal of Molecular Biology, 1990
- Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 Å resolutionJournal of Molecular Biology, 1990