1RBL

STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301

Summary for 1RBL

• Entry DOI: 10.2210/pdb1rbl/pdb
• Descriptor: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE CHAIN), RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL CHAIN), MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: lyase(carbon-carbon), lyase
• Biological source: Synechococcus elongatus; More
• Total number of polymer chains: 16
• Total formula weight: 521799.42

Authors

Newman, J.,Gutteridge, S.,Branden, C.-I.,Jones, T.A. (deposition date: 1993-05-12, release date: 1994-06-22, Last modification date: 2024-06-05)

Primary citation

Newman, J.,Branden, C.I.,Jones, T.A.
Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301.
Acta Crystallogr.,Sect.D, 49:548-560, 1993

PubMed Abstract: The structure of an activated quaternary complex of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus PCC6301 has been solved by molecular replacement. The protein crystallizes in an orthorhombic P2(1)2(1)2(1) unit cell with a complete L(8)S(8) complex consisting of 4608 residues (37 680 non-hydrogen atoms) in the asymmetric unit. Data were collected both on film and image plate using synchrotron radiation; there were 218 276 unique reflections in the final 2.2 A data set. The eightfold non-crystallographic symmetry could be used both to improve map quality and to reduce the computing requirements of refinement. The coordinates were refined using strict non-crystallographic symmetry constraints. The stereochemistry of the final model is good, and the model has an R value of 20.0% for the reflections between 7 and 2.2 A.

PubMed: 15299492
DOI: 10.1107/S090744499300530X

Experimental method

X-RAY DIFFRACTION (2.2 Å)