1plc
From Proteopedia
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ACCURACY AND PRECISION IN PROTEIN CRYSTAL STRUCTURE ANALYSIS: RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF POPLAR PLASTOCYANIN AT 1.33 ANGSTROMS RESOLUTION
Overview
The structure of the electron-transfer protein, plastocyanin (99 amino, acids, one Cu atom, 10,500 Da) from poplar leaves, has been refined at, 1.33 A resolution to a residual R = 0.15. The space group is orthorhombic, P2(1)2(1)2(1), a = 29.60 (1), b = 46.86 (3), c = 57.60 (3) A. The 14,303, reflections used in the refinement were obtained from a data set recorded, on a four-circle diffractometer with radiation from a sealed fine-focus, tube, combined with a data set measured on oscillation films exposed at, the DESY synchrotron. The final model comprises 1442 (738 non-H) protein, atoms, one Cu atom and 110 solvent molecules. Nine residues are described, as disordered. The root-mean-square deviation from ideal bond lengths is, 0.016 A and the root-mean-square difference between the positions of the C, alpha atoms in this refined model and in the structure previously refined, at 1.6 A resolution is 0.11 A. The effects of manual model adjustment, resolution, choice of standard values for geometrical parameters, inclusion of H atoms and inclusion of anomalous-scattering corrections on, the copper-site geometry have been explored. The final values of the, Cu-ligand bond lengths are: Cu--N(His37) 1.91, Cu--S(Cys84) 2.07, Cu--N(His87) 2.06, Cu--S(Met92) 2.82 A.
About this Structure
1PLC is a Single protein structure of sequence from Populus nigra with CU as ligand. This structure superseeds the now removed PDB entry 1PCY. Full crystallographic information is available from OCA.
Reference
Accuracy and precision in protein structure analysis: restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 A resolution., Guss JM, Bartunik HD, Freeman HC, Acta Crystallogr B. 1992 Dec 1;48 ( Pt 6):790-811. PMID:1492962
Page seeded by OCA on Tue Nov 20 23:54:34 2007
