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

TitleCombining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin.
Publication TypeJournal Article
Year of Publication2006
AuthorsRoos, G., E. Brosens, K. Wahni, A. Desmyter, S. Spinelli, L. Wyns, J. Messens, and R. Loris
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume62
IssuePt 12
Pagination1255-8
Date Published2006 Dec 1
ISSN1744-3091
KeywordsCrystallization, Crystallography, X-Ray, Mutagenesis, Site-Directed, Staphylococcus aureus, Thioredoxins
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.
DOI10.1107/S1744309106047075
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID17142910
PubMed Central IDPMC2225371
subject_category: 
Redox
Research group: 
MessensGroup