Literature DB >> 19052376

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

Kerstin Steiner1, Anna Wojciechowska, Christina Schäffer, James H Naismith.   

Abstract

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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Year:  2008        PMID: 19052376      PMCID: PMC2593710          DOI: 10.1107/S1744309108036762

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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Journal:  J Mol Biol       Date:  2010-01-22       Impact factor: 5.469

  2 in total

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