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

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Title: Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum.
Authors: Kovalevsky, Andrey Y., Hanson, B. Leif, Seaver, Sean, Fisher, S. Zoë, Mustyakimov, Marat, Langan, Paul
Source: Acta Crystallographica: Section F (Wiley-Blackwell). Feb2011, Vol. 67 Issue 2, p283-286. 4p.
Subjects: Trichoderma, Neutron diffraction crystallography, Xylanases, Biomass energy, Crystals
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. [ABSTRACT FROM AUTHOR]
Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
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  Data: <searchLink fieldCode="DE" term="%22Trichoderma%22">Trichoderma</searchLink><br /><searchLink fieldCode="DE" term="%22Neutron+diffraction+crystallography%22">Neutron diffraction crystallography</searchLink><br /><searchLink fieldCode="DE" term="%22Xylanases%22">Xylanases</searchLink><br /><searchLink fieldCode="DE" term="%22Biomass+energy%22">Biomass energy</searchLink><br /><searchLink fieldCode="DE" term="%22Crystals%22">Crystals</searchLink>
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  Data: 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1107/S174430911005075X
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        Text: English
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        Type: general
      – SubjectFull: Neutron diffraction crystallography
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      – SubjectFull: Xylanases
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      – SubjectFull: Biomass energy
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              Text: Feb2011
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