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, Silvia Spinelli, Aline Desmyter, Lode Wyns, Joris Messens, Remy Loris

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Abstract The P31T mutant of Staphylococcus aureus thioredoxin crystallizes spontaneously in space group P212121 with unit cell parameters a = 41.7 Å, b = 49.5 Å, c=55.6 Å. The crystals diffract to 2.2 Å resolution. Isomorphous crystals of wild type thioredoxin as well as of other point mutants only grow when seeded with the P31T mutant. Our 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 Crystallogr F Struct Biol Commun
Volume62
Publication statusPublished - Dec 2006

Keywords

  • macromolecular crystallography

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