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Journal of Virology|April 9, 2010
Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assemblyThomas A Bowden, Max Crispin, David J Harvey, et al.
Nature|May 12, 2006
A mechanical explanation of RNA pseudoknot function in programmed ribosomal frameshiftingOlivier Namy, Stephen J Moran, David I Stuart, et al.
Plos Biology|February 18, 2010
Using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complexChristian H Bell, Steven L Porter, Annabel Strawson, et al.
Acta Crystallographica. Section D, Biological Crystallography|September 25, 2004
Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBISanna Askolin, Johan P Turkenburg, Maija Tenkanen, et al.
Acta Crystallographica. Section D, Biological Crystallography|September 9, 2010
The structure of the genomic Bacillus subtilis dUTPase: novel features in the Phe-lidJavier García-Nafría, Lynn Burchell, Mine Takezawa, et al.
Acta Crystallographica. Section F, Structural Biology Communications|January 24, 2015
The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 Å resolutionOlga V Moroz, Michelle Maranta, Tarana Shaghasi, et al.
Chemical Communications (Cambridge, England)|September 2, 2008
Petrobactin biosynthesis: AsbB catalyzes condensation of spermidine with N8-citryl-spermidine and its N1-(3,4-dihydroxybenzoyl) derivativeDaniel Oves-Costales, Nadia Kadi, Mark J Fogg, et al.
The Journal of Biological Chemistry|April 17, 2013
Crystal and solution studies reveal that the transcriptional regulator AcnR of Corynebacterium glutamicum is regulated by citrate-Mg2+ binding to a non-canonical pocketJavier García-Nafría, Meike Baumgart, Johan P Turkenburg, et al.
Structure (London, England : 1993)|June 15, 2010
Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin familyJitka Vévodová, Michael Gamble, Georg Künze, et al.
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