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Crystallization and preliminary X-ray crystallographic analysis of Sulfolobus solfataricus thioredoxin reductase.


ABSTRACT: A thermostable thioredoxin reductase isolated from Sulfolobus solfataricus (SsTrxR) has been successfully crystallized in the absence and in the presence of NADP. Two different crystal forms have been obtained. Crystals of the form that yields higher resolution data (1.8 A) belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.77, b = 120.68, c = 126.85 A. The structure of the enzyme has been solved by MAD methods using the anomalous signal from the Se atoms of selenomethionine-labelled SsTrxR.

SUBMITTER: Ruggiero A 

PROVIDER: S-EPMC1991316 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of Sulfolobus solfataricus thioredoxin reductase.

Ruggiero Alessia A   Ruocco Maria Rosaria MR   Grimaldi Pasquale P   Arcari Paolo P   Masullo Mariorosario M   Zagari Adriana A   Vitagliano Luigi L  

Acta crystallographica. Section F, Structural biology and crystallization communications 20050930 Pt 10


A thermostable thioredoxin reductase isolated from Sulfolobus solfataricus (SsTrxR) has been successfully crystallized in the absence and in the presence of NADP. Two different crystal forms have been obtained. Crystals of the form that yields higher resolution data (1.8 A) belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.77, b = 120.68, c = 126.85 A. The structure of the enzyme has been solved by MAD methods using the anomalous signal from the Se atoms of selenomethionine-l  ...[more]

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