Crystallization of mutant forms of glutaredoxin Grx1p from yeast
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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 Å (synchrotron radiation) and 2.7 Å (rotating-anode generator), respectively. In contrast, rxYFP-Grx1p formed crystals at high pH in MgSO4 which diffract synchrotron radiation to 2.7 Å.
Original language | English |
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Journal | Acta Crystallographica. Section F : Structural Biology and Crystallization Communications |
Volume | 62 |
Issue number | 9 |
Pages (from-to) | 920-922 |
ISSN | 1744-3091 |
DOIs | |
Publication status | Published - 2006 |
Bibliographical note
glutaredoxins; Grx1p; yellow fluorescent protein.
ID: 1557997