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Crystallization of mutant forms of glutaredoxin Grx1p from yeast.

ABSTRACT: Glutaredoxin Grx1p from yeast was crystallized both as an independent protein and in a protein fusion with His-tagged yellow fluorescent protein (rxYFP). A glutathionylated C30S mutant of the 12 kDa Grx1p was crystallized in two different forms in PEG 4000 at low pH. These orthorhombic and monoclinic forms diffract to 2.0 A (synchrotron radiation) and 2.7 A (rotating-anode generator), respectively. In contrast, rxYFP-Grx1p formed crystals at high pH in MgSO(4) which diffract synchrotron radiation to 2.7 A.

SUBMITTER: Hakansson KO

PROVIDER: S-EPMC2242864 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature

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Crystallization of mutant forms of glutaredoxin Grx1p from yeast.

Håkansson Kjell O KO Østergaard Henrik H Winther Jakob R JR

Acta crystallographica. Section F, Structural biology and crystallization communications 20060826 Pt 9

Glutaredoxin Grx1p from yeast was crystallized both as an independent protein and in a protein fusion with His-tagged yellow fluorescent protein (rxYFP). A glutathionylated C30S mutant of the 12 kDa Grx1p was crystallized in two different forms in PEG 4000 at low pH. These orthorhombic and monoclinic forms diffract to 2.0 A (synchrotron radiation) and 2.7 A (rotating-anode generator), respectively. In contrast, rxYFP-Grx1p formed crystals at high pH in MgSO(4) which diffract synchrotron radiatio ...[more]

PMID: 16946480

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