Neutron crystallographic study on rubredoxin from Pyrococcus furiosus by BIX-3, a single-crystal diffractometer for biomacromolecules. - Wikidata - awgldk - TriplyDB

Neutron crystallographic study on rubredoxin from Pyrococcus furiosus by BIX-3, a single-crystal diffractometer for biomacromolecules.

Neutron crystallographic study on rubredoxin from Pyrococcus furiosus by BIX-3, a single-crystal diffractometer for biomacromolecules.

http://www.wikidata.org/entity/Q37388518

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Complicated water orientations in the minor groove of the B-DNA decamer d(CCATTAATGG)2 observed by neutron diffraction measurements Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa Neutron and X-ray structural studies of short hydrogen bonds in photoactive yellow protein (PYP)Rapid visualization of hydrogen positions in protein neutron crystallographic structures Near-atomic resolution neutron crystallography on perdeuterated Pyrococcus furiosus rubredoxin: implication of hydronium ions and protonation state equilibria in redox changes The IMAGINE instrument: first neutron protein structure and new capabilities for neutron macromolecular crystallography Perdeuteration: improved visualization of solvent structure in neutron macromolecular crystallography Joint X-ray and neutron refinement with phenix.refine.Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate.Assessing the chemical accuracy of protein structures via peptide acidity.Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris.Neutron crystallography: opportunities, challenges, and limitations Generalized X-ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules Getting protein solvent structures down cold.Regulation of iron metabolism by Pyrococcus furiosus.

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P2860

Neutron crystallographic study on rubredoxin from Pyrococcus furiosus by BIX-3, a single-crystal diffractometer for biomacromolecules.

http://www.wikidata.org/entity/Q37388518

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 22 July 2004

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Neutron crystallographic study ...... tometer for biomacromolecules.

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Neutron crystallographic study ...... tometer for biomacromolecules.

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Neutron crystallographic study ...... tometer for biomacromolecules.

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Neutron crystallographic study ...... tometer for biomacromolecules.

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Neutron crystallographic study ...... tometer for biomacromolecules.

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Neutron crystallographic study ...... tometer for biomacromolecules.

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PNAS.0403807101

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Proceedings of the National Academy of Sciences of the United States of America

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Neutron crystallographic study ...... tometer for biomacromolecules.

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P2093

Francis E Jenney

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Ichiro Tanaka

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Kazuo Kurihara

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Michael W W Adams

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Natalia Moiseeva

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Nobuo Niimura

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Robert Bau

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Toshiyuki Chatake

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P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme

Direct determination of the positions of the deuterium atoms of the bound water in -concanavalin A by neutron Laue crystallography

A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism

Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 A resolution

X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

Solution-state structure by NMR of zinc-substituted rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution

Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 A resolution

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scholarly article

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10.1073/PNAS.0403807101

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2004-07-22T00:00:00Z

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