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

X. Li; P. Langan; R. Bau; I. Tsyba; Francis E. Jenney; Michael W. Adams; B. P. Schoenborn

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

X. Li, P. Langan, R. Bau, I. Tsyba, Francis E. Jenney, Michael W. Adams, B. P. Schoenborn

Department of Bio-Medical Sciences (PCOM)

Research output: Contribution to journal › Article › peer-review

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	American English
Journal	Acta crystallographica.Section D, Biological crystallography
Volume	60
State	Published - Jan 1 2004

Disciplines

Biochemistry, Biophysics, and Structural Biology

Cite this

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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.",

author = "X. Li and P. Langan and R. Bau and I. Tsyba and Jenney, {Francis E.} and Adams, {Michael W.} and Schoenborn, {B. P.}",

year = "2004",

month = jan,

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language = "American English",

volume = "60",

journal = "Acta crystallographica.Section D, Biological crystallography",

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TY - JOUR

T1 - W3Y single mutant of rubredoxin from Pyrococcus furiosus: a preliminary time-of-flight neutron study.

AU - Li, X.

AU - Langan, P.

AU - Bau, R.

AU - Tsyba, I.

AU - Jenney, Francis E.

AU - Adams, Michael W.

AU - Schoenborn, B. P.

PY - 2004/1/1

Y1 - 2004/1/1

N2 - 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.

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.

UR - https://digitalcommons.pcom.edu/scholarly_papers/624

M3 - Article

VL - 60

JO - Acta crystallographica.Section D, Biological crystallography

JF - Acta crystallographica.Section D, Biological crystallography

ER -

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

Abstract

Disciplines

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