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Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum

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...

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Hlavní autoři: Kovalevsky, Andrey Y., Hanson, B. Leif, Seaver, Sean, Fisher, S. Zoë, Mustyakimov, Marat, Langan, Paul
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2011
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3034629/
https://ncbi.nlm.nih.gov/pubmed/21301107
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S174430911005075X
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