1rbl
From Proteopedia
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==Overview== | ==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 ... | + | 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== | ==About this Structure== | ||
| - | 1RBL is a | + | 1RBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with MG, CAP and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] Structure known Active Site: 1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RBL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lyase(carbon-carbon)]] | [[Category: lyase(carbon-carbon)]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:31:47 2007'' |
Revision as of 10:26, 5 November 2007
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STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301
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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