1992Protein ScienceOpen access

Comparison of the X‐ray structure of native rubredoxin from pyrococcus furiosus with the NMR structure of the zinc‐substituted protein

Paul R. Blake, Michael W. Day, Barbara T. Hsu, Leemor Joshua‐Tor, Jae‐Bum Park, Dennis R. Hare, Michael W. W. Adams, Douglas C. Rees, Michael F. Summers

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Abstract

The three-dimensional X-ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at -161 degrees C, and the NMR structure of the zinc-substituted protein, determined in solution at 45 degrees C, are compared. The NMR and X-ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.

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What this paper is about

The three-dimensional X-ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at -161 degrees C, and the NMR structure of the zinc-substituted protein, determined in solution at 45 degrees C, are compared. The NMR and X-ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.

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Available abstract

The three-dimensional X-ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at -161 degrees C, and the NMR structure of the zinc-substituted protein, determined in solution at 45 degrees C, are compared. The NMR and X-ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.

Key concepts: Rubredoxin, Pyrococcus furiosus, Crystallography, Zinc, Chemistry, Protein structure, Zinc finger, Biochemistry

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Comparison of the X‐ray structure of native rubredoxin from pyrococcus furiosus with the NMR structure of the zinc‐substituted protein — Research Paper | ScholarLens