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. 2006 Dec 1;62(Pt 12):1255-8.
doi: 10.1107/S1744309106047075. Epub 2006 Nov 30.

Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin

Goedele Roos  1 , Elke Brosens, Khadija Wahni, Aline Desmyter, Silvia Spinelli, Lode Wyns, Joris Messens, Remy Loris
Affiliations

Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin

Goedele Roos et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

The P31T mutant of Staphylococcus aureus thioredoxin crystallizes spontaneously in space group P2(1)2(1)2(1), with unit-cell parameters a = 41.7, b = 49.5, c = 55.6 A. The crystals diffract to 2.2 A resolution. Isomorphous crystals of wild-type thioredoxin as well as of other point mutants only grow when seeded with the P31T mutant. These results suggest seeding as a valuable tool complementing surface engineering for proteins that are hard to crystallize.

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Figures

Figure 1
Figure 1
Typical crystals of Sa_Trx P31T.
Figure 2
Figure 2
Diffraction pattern of wild-type Sa_Trx.
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