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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization of mutant forms of glutaredoxin Grx1p from yeast.

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.[1]

References

  1. Crystallization of mutant forms of glutaredoxin Grx1p from yeast. Håkansson, K.O., Østergaard, H., Winther, J.R. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
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