W3Y single mutant of rubredoxin from Pyrococcus furiosus: a preliminary time-of-flight neutron study.

Xinmin Li; Paul Langan; Robert Bau; Irina Tsyba; Francis E. Jenney; Michael W.W. Adams; Benno P. Schoenborn

doi:10.1107/S0907444903024041

W3Y single mutant of rubredoxin from Pyrococcus furiosus: a preliminary time-of-flight neutron study.

Xinmin Li, Paul Langan, Robert Bau, Irina Tsyba, Francis E. Jenney, Michael W.W. Adams, Benno P. Schoenborn

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19 Scopus citations

Abstract

Rubredoxin from the hyperthermophilic archaeon Pyrococcus furiosus maintains its native structure at high temperatures (373 K). In order to investigate the role of hydrogen bonding, hydration and chain dynamics in this thermostability, wavelength-resolved Laue neutron diffraction data have been collected from the W3Y single mutant (Trp3-->Tyr3) on the spallation neutron protein crystallography station (PCS) at Los Alamos Neutron Science Center. Data were measured at room temperature from nine crystal settings, each of approximately 12 h duration. The total data-measurement period was less than 5 d from a single crystal that had undergone H(2)O/D(2)O exchange. The nominal resolution of the data is 2.1 A.

Original language	English
Pages (from-to)	200-202
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	60
Issue number	Pt 1
DOIs	https://doi.org/10.1107/S0907444903024041
State	Published - Jan 2004
Externally published	Yes

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title = "W3Y single mutant of rubredoxin from Pyrococcus furiosus: a preliminary time-of-flight neutron study.",

abstract = "Rubredoxin from the hyperthermophilic archaeon Pyrococcus furiosus maintains its native structure at high temperatures (373 K). In order to investigate the role of hydrogen bonding, hydration and chain dynamics in this thermostability, wavelength-resolved Laue neutron diffraction data have been collected from the W3Y single mutant (Trp3-->Tyr3) on the spallation neutron protein crystallography station (PCS) at Los Alamos Neutron Science Center. Data were measured at room temperature from nine crystal settings, each of approximately 12 h duration. The total data-measurement period was less than 5 d from a single crystal that had undergone H(2)O/D(2)O exchange. The nominal resolution of the data is 2.1 A.",

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AU - Li, Xinmin

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AU - Bau, Robert

AU - Tsyba, Irina

AU - Jenney, Francis E.

AU - Adams, Michael W.W.

AU - Schoenborn, Benno P.

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AB - Rubredoxin from the hyperthermophilic archaeon Pyrococcus furiosus maintains its native structure at high temperatures (373 K). In order to investigate the role of hydrogen bonding, hydration and chain dynamics in this thermostability, wavelength-resolved Laue neutron diffraction data have been collected from the W3Y single mutant (Trp3-->Tyr3) on the spallation neutron protein crystallography station (PCS) at Los Alamos Neutron Science Center. Data were measured at room temperature from nine crystal settings, each of approximately 12 h duration. The total data-measurement period was less than 5 d from a single crystal that had undergone H(2)O/D(2)O exchange. The nominal resolution of the data is 2.1 A.

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W3Y single mutant of rubredoxin from Pyrococcus furiosus: a preliminary time-of-flight neutron study.

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