Purification, crystallization and preliminary crystallographic analysis of WsaF, an essential rhamnosyltransferase from Geobacillus stearothermophilus.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, Scotland.

Published: December 2008

The beta1,2-rhamnosyltransferase WsaF is involved in the biosynthesis of a polyrhamnan chain which is attached to the surface-layer protein from Geobacillus stearothermophilus NRS 2004/3a. The enzyme belongs to the large retaining GT4 family. To date, no structure of a rhamnosyltransferase has been published. Recombinant purified native WsaF has been crystallized, resulting in crystals that belonged to space group P2(1)2(1)2(1) with unit-cell parameters a = 50.5, b = 56.1, c = 276.8 A and diffracted to 3.0 A resolution. Selenomethionine-variant WsaF crystallized in space group P2(1) with unit-cell parameters a = 75.9, b = 75.5, c = 78.1 A and diffracted to 2.3 A resolution.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2593710PMC
http://dx.doi.org/10.1107/S1744309108036762DOI Listing

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