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

Publication Type:

Journal Article

Authors:

Roos,G.; Brosens,E.; Wahni,K.; Desmyter,A.; Spinelli,S.; Wyns,L.; Messens,J.; Loris,R.

Source:

Acta Crystallogr. Sect F Struct. Biol. Cryst. Commun., Volume 62, Issue Pt 12, p.1255 - 1258 (2006)

URL:

PM:17142910

Keywords:

Crystallization; methods; Crystallography; X-Ray; Mutagenesis; Site-Directed; Staphylococcus aureus; chemistry; genetics; Thioredoxins; isolation & purification

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

Notes:

DA - 20061204
IS - 1744-3091 (Electronic)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 52500-60-4 (Thioredoxins)
SB - IM