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

Document Type

Article

Publication Date

2004

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.

Publication Title

Acta crystallographica.Section D, Biological crystallography

Volume

60

First Page

200

Last Page

202

Comments

This article was published in Acta crystallographica.Section D, Biological crystallography, Volume 60, Issue Pt 1, Pages 200-202.

The published version is available at http://dx.doi.org/ .

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