1rbl | pdb_00001rbl
STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301
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Overview
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.
About this Structure
1RBL is a Protein complex structure of sequences from Synechococcus sp. with MG, CAP and FMT as ligands. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Structure known Active Site: 1. Full crystallographic information is available from OCA.
Reference
Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301., Newman J, Branden CI, Jones TA, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):548-60. PMID:15299492
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