ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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3 citing papers in PubMed, 7 citations in OpenAlex.
- Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Heterologous expression, purification, crystallization and preliminary X-ray analysis of Trichoderma reesei xylanase II and four variants.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Crystals on the cover 2012.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Room-temperature X-ray and neutron diffraction data were measured from a family 11 endoxylanase holoenzyme (XynII) originating from the filamentous fungus Trichoderma longibrachiatum to 1.55 Å resolution using a home source and to 1.80 Å resolution using the Protein Crystallography Station at LANSCE. Crystals of XynII, which is an important enzyme for biofuel production, were grown at pH 8.5 in order to examine the effect of basic conditions on the protonation-state distribution in the active site and throughout the protein molecule and to provide insights for rational engineering of catalytically improved XynII for industrial applications.
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