W3Y single mutant of rubredoxin from Pyrococcus furiosus: a preliminary time-of-flight neutron study.
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.
Li
Xinmin
X
Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Langan
Paul
P
Bau
Robert
R
Tsyba
Irina
I
Jenney
Francis E
FE
Adams
Michael W W
MW
Schoenborn
Benno P
BP
D003460:Crystallization; D003903:Deuterium; D033363:Neutron Diffraction; D017354:Point Mutation; D020027:Pyrococcus furiosus / Q000737:chemistry*; D012416:Rubredoxins / Q000737:chemistry*
D012416:Rubredoxins; D003903:Deuterium