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REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS

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Standard

REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS. / DAUTER, Z ; SIEKER, L C ; WILSON, K S .

In: ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE, Vol. 48, 01.02.1992, p. 42-59.

Research output: Contribution to journalArticlepeer-review

Harvard

DAUTER, Z, SIEKER, LC & WILSON, KS 1992, 'REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS', ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE, vol. 48, pp. 42-59.

APA

DAUTER, Z., SIEKER, L. C., & WILSON, K. S. (1992). REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS. ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE, 48, 42-59.

Vancouver

DAUTER Z, SIEKER LC, WILSON KS. REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS. ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE. 1992 Feb 1;48:42-59.

Author

DAUTER, Z ; SIEKER, L C ; WILSON, K S . / REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS. In: ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE. 1992 ; Vol. 48. pp. 42-59.

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@article{60eb62d0f29442edad339ce6a159a8fd,
title = "REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 {\AA} WITH AND WITHOUT RESTRAINTS",
abstract = "X-ray data have been recorded from crystals of rubredoxin derived from the bacterium Desulfovibrio vulgaris to a resolution of 1.0 angstrom using in part synchrotron radiation and in part X-rays from a sealed-tube Mo K-alpha source. In both cases an imaging-plate scanner was used as detector. The space group of the crystals is P2(1) with cell dimensions a = 19.97, b = 41.45, c = 24.41 angstrom and beta = 108.3-degrees. The overall merging R(I) factor between symmetry-related reflections was 5.8%. The model was refined by least-squares minimization initially with stereochemical restraints to an R factor of 16.4%. Only atomic positional parameters and isotropic temperature factors for non-H atoms were used in the refinement. There were 18 532 independent X-ray observations for a total of 1916 atomic parameters. A round of unrestrained refinement gave an R factor of 16.0%, acceptable geometry for more than 90% of the protein atoms, but emphasized the disorder inherent in eight of the residues. A final round of restrained refinement gave an R factor of 14.7%. Three of the 389 protein atoms in the molecule, in the side chain of Lys2, have been assigned zero occupancy in the model. A total of eight atoms in three side chains have been assigned two conformations, giving 393 protein atomic sites in the model. In addition there is one Fe atom, a sulfate ion and 102 water sites. 339 H atoms were included at their calculated positions, which were not refined. There is clear evidence for anisotropic thermal motion. This has not been incorporated in the present model.",
author = "Z DAUTER and SIEKER, {L C} and WILSON, {K S}",
year = "1992",
month = feb,
day = "1",
language = "English",
volume = "48",
pages = "42--59",
journal = "ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE",
issn = "0108-7681",
publisher = "International Union of Crystallography",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - REFINEMENT OF RUBREDOXIN FROM DESULFOVIBRIO VULGARIS AT 1.0 Å WITH AND WITHOUT RESTRAINTS

AU - DAUTER, Z

AU - SIEKER, L C

AU - WILSON, K S

PY - 1992/2/1

Y1 - 1992/2/1

N2 - X-ray data have been recorded from crystals of rubredoxin derived from the bacterium Desulfovibrio vulgaris to a resolution of 1.0 angstrom using in part synchrotron radiation and in part X-rays from a sealed-tube Mo K-alpha source. In both cases an imaging-plate scanner was used as detector. The space group of the crystals is P2(1) with cell dimensions a = 19.97, b = 41.45, c = 24.41 angstrom and beta = 108.3-degrees. The overall merging R(I) factor between symmetry-related reflections was 5.8%. The model was refined by least-squares minimization initially with stereochemical restraints to an R factor of 16.4%. Only atomic positional parameters and isotropic temperature factors for non-H atoms were used in the refinement. There were 18 532 independent X-ray observations for a total of 1916 atomic parameters. A round of unrestrained refinement gave an R factor of 16.0%, acceptable geometry for more than 90% of the protein atoms, but emphasized the disorder inherent in eight of the residues. A final round of restrained refinement gave an R factor of 14.7%. Three of the 389 protein atoms in the molecule, in the side chain of Lys2, have been assigned zero occupancy in the model. A total of eight atoms in three side chains have been assigned two conformations, giving 393 protein atomic sites in the model. In addition there is one Fe atom, a sulfate ion and 102 water sites. 339 H atoms were included at their calculated positions, which were not refined. There is clear evidence for anisotropic thermal motion. This has not been incorporated in the present model.

AB - X-ray data have been recorded from crystals of rubredoxin derived from the bacterium Desulfovibrio vulgaris to a resolution of 1.0 angstrom using in part synchrotron radiation and in part X-rays from a sealed-tube Mo K-alpha source. In both cases an imaging-plate scanner was used as detector. The space group of the crystals is P2(1) with cell dimensions a = 19.97, b = 41.45, c = 24.41 angstrom and beta = 108.3-degrees. The overall merging R(I) factor between symmetry-related reflections was 5.8%. The model was refined by least-squares minimization initially with stereochemical restraints to an R factor of 16.4%. Only atomic positional parameters and isotropic temperature factors for non-H atoms were used in the refinement. There were 18 532 independent X-ray observations for a total of 1916 atomic parameters. A round of unrestrained refinement gave an R factor of 16.0%, acceptable geometry for more than 90% of the protein atoms, but emphasized the disorder inherent in eight of the residues. A final round of restrained refinement gave an R factor of 14.7%. Three of the 389 protein atoms in the molecule, in the side chain of Lys2, have been assigned zero occupancy in the model. A total of eight atoms in three side chains have been assigned two conformations, giving 393 protein atomic sites in the model. In addition there is one Fe atom, a sulfate ion and 102 water sites. 339 H atoms were included at their calculated positions, which were not refined. There is clear evidence for anisotropic thermal motion. This has not been incorporated in the present model.

M3 - Article

VL - 48

SP - 42

EP - 59

JO - ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE

JF - ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE

SN - 0108-7681

ER -