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

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

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)1255-1258
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue numberPt 12
DOIs
Publication statusPublished - 1 Dec 2006

Keywords

  • Crystallization
  • Crystallography, X-Ray
  • Mutagenesis, Site-Directed
  • Staphylococcus aureus
  • Thioredoxins
  • Journal Article
  • Research Support, Non-U.S. Gov't

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