Crystallization and preliminary X-ray crystallographic studies of XynX, a family 10 xylanase from Aeromonas punctata ME-1

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Zui FujimotoTohru Suzuki

Abstract

Xylanases catalyze the hydrolysis of beta-1,4-glycosidic linkages within the xylan backbone. XynX is a xylanase from Aeromonas punctata ME-1 and belongs to glycoside hydrolase family 10. While most xylanases show endo-type catalytic activities, XynX shows exo-like catalytic activities, selectively producing xylobiose from birchwood xylan. In this study, XynX was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 79.0, b = 88.6, c = 93.2 A, and diffracted to beyond 1.8 A resolution.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Jul 1, 1995·Nature Structural Biology·R DominguezP M Alzari
Oct 29, 1998·Protein Science : a Publication of the Protein Society·A SchmidtC Kratky
Apr 23, 2004·Acta Crystallographica. Section D, Biological Crystallography·A TeplitskyG Shoham

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cardiac Glycosides

Cardiac glycosides are a diverse family of naturally derived compounds that bind to and inhibit na+/k+-atpase. Discover the latest research on cardiac glycosides heres.

Related Papers

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
K ManikandanS Ramakumar
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Takuya IshidaMasahiro Samejima
Acta Crystallographica. Section D, Biological Crystallography
Zui FujimotoHiroshi Mizuno
Acta Crystallographica. Section D, Biological Crystallography
IhsanawatiNobuo Tanaka
© 2021 Meta ULC. All rights reserved