𝔖 Bobbio Scriptorium
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Purification and characterization of two xylanases from Trichoderma longibrachiatum

✍ Scribed by John C. ROYER; James P. NAKAS

Book ID
115128902
Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
823 KB
Volume
202
Category
Article
ISSN
1432-1327

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πŸ“œ SIMILAR VOLUMES

Solution scattering studies of conformat
Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum
✍ Maciej Kozak πŸ“‚ Article πŸ“… 2006 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 288 KB

## Abstract Xylanase (__endo__‐1,4‐β‐xylanase; EC 3.2.1.8) is an enzyme that catalyzes the hydrolysis reaction of xylan. The structure of the xylanase II (XYNII) molecule from __Trichoderma longibrachoatum__ (formerly __Trichoderma reesei__) in a solution and at different pH values has been studied

Using barium ions for heavy-atom derivat
Using barium ions for heavy-atom derivatization and phasing of xylanase II from Trichoderma longibrachiatum
✍ Moiseeva, Natalia ;Allaire, Marc πŸ“‚ Article πŸ“… 2007 πŸ› International Union of Crystallography 🌐 English βš– 468 KB

This paper describes the use of barium chloride to produce a heavy-atom derivative of xylanase II crystals from Trichoderma longibrachiatum, which was obtained either by cocrystallization or soaking. SAD phasing led to interpretable electron-density maps that allowed unambiguous chain tracing. In th