ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Purification, crystallization and preliminary crystallographic analysis of WsaF, an essential rhamnosyltransferase from Geobacillus stearothermophilus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 3 citations in OpenAlex.
- The s-layer glycome-adding to the sugar coat of bacteria.International journal of microbiology · 2011Article
- Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus.Journal of molecular biology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
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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