Staphylococcus Research Today is a free monthly online journal that collates and summarizes the latest research about Staphylococcus, including details on mrsa, hospitals, infection, antibiotic resistance, superbugs.

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

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

Brussels Center for Redox Biology, Vlaams Interuniversitair Instituut voor Biotechnologie at the Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium.

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.

Published 4 December 2006 in Acta Crystallograph Sect F Struct Biol Cryst Commun, 62: 1255-8.
Full-text of this article is available online (may require subscription).

© 2004-2008 Staphylococcus Research Today. All Rights Reserved.