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Titolo:
ACCURACY AND PRECISION IN PROTEIN CRYSTAL-STRUCTURE ANALYSIS - 2 INDEPENDENT REFINEMENTS OF THE STRUCTURE OF POPLAR PLASTOCYANIN AT 173-K
Autore:
FIELDS BA; BARTSCH HH; BARTUNIK HD; CORDES F; GUSS JM; FREEMAN HC;
Indirizzi:
UNIV SYDNEY,DEPT INORGAN CHEM SYDNEY NSW 2006 AUSTRALIA DESY,MAX PLANCK RES UNIT STRUCT MOLEC BIOL D-22603 HAMBURG GERMANY
Titolo Testata:
Acta crystallographica. Section D, Biological crystallography
, volume: 50, anno: 1994,
parte:, 5
pagine: 709 - 730
SICI:
0907-4449(1994)50:<709:AAPIPC>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESONANCE RAMAN-SPECTRA; BLUE COPPER PROTEINS; CRYSTALLOGRAPHIC REFINEMENT; CRYOGENIC TEMPERATURES; ELECTRONIC-STRUCTURE; RESOLUTION; FEATURES; SITE; MOLECULES; DYNAMICS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
B.A. Fields et al., "ACCURACY AND PRECISION IN PROTEIN CRYSTAL-STRUCTURE ANALYSIS - 2 INDEPENDENT REFINEMENTS OF THE STRUCTURE OF POPLAR PLASTOCYANIN AT 173-K", Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 709-730

Abstract

The structure of the copper protein plastocyanin from poplar leaves (Populus nigra var. italica) at 173 K has been subjected to two independent refinements, using a single set of synchrotron X-ray data at 1.6 angstrom resolution. Energy-restrained refinement using the program EREF resulted in lower root-mean-square deviations from ideal geometry (e.g. 0.011 angstrom for bond lengths) but a higher residual R (0.153) than restrained least-squares refinement using the program PROLSQ (0.014 angstrom, 0.132). Electron-density difference maps in both refinements provided evidence for disorder at some side chains and solvent atoms, and the PROLSQ refinement made allowance for this disorder. The number of solvent sites identified at the 4sigma(rho) level was 171 in the EREF refinement and 189 in the PROLSQ refinement; 159 of the solvent sites are common to both refinements within 1 angstrom. The root-mean-square differences between the atomic positions produced by the two refinements are 0.08 angstrom for C(alpha) atoms, 0.08 angstrom for backbone atoms and 0.12 angstrom for all non-H atoms (excluding six obvious outliers) of the protein molecule. The two sets of Cu-ligand bond lengths differ by up to 0.07 angstrom, and the ligand-Cu-ligand anglesby up to 7-degrees. At 173 K the volume of the unit cell is 4.2% smaller than at 295 K. Greater order in the solvent region is indicated bythe location of 79 more solvent sites, the identification of extensive networks of hydrogen-bonded rings of solvent molecules, and a general decrease in the thermal parameters. Within the unit cell, the protein molecules are significantly translated and rotated from their positions at ambient temperature. An important structural change at low temperature is a 180-degrees flip of the peptide group at Ser48-Gly49. Nearly all other significant differences between the structures of the protein at 173 and 295 K occur at exposed side chains. If the backbone atoms in the 173 and 295 K structures are superposed, excluding atoms involved in the peptide flip, the root-mean-square difference between the positions of 393 atoms is 0.25 angstrom. Two internal water molecules, not included in previous descriptions of poplar plastocyanin, havebeen located. The plastocyanin Cu-site geometry at 173 K is not significantly different from that at 295 K. If plastocyanin undergoes a change in Cu-site geometry at low temperature, as has been suggested on the basis of resonance Raman spectroscopic evidence, then the change isnot detected within the limits of precision of the present results.

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