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Xylanase B From Clostridium Cellulovorans 743B: Overexpression, Purification, Crystallization and X-ray Diffraction Analysis

Xylanase B From Clostridium Cellulovorans 743B: Overexpression, Purification, Crystallization and X-ray Diffraction Analysis

Daichi Nakajima, Akihiko Nagano, Toshiyuki Shibata, Reiji Tanaka, Kouichi Kuroda, Mitsuyoshi Ueda, Hideo Miyake

Acta Crystallogr F Struct Biol Commun. 2018 Feb 1;74(Pt 2):113-116.

PMID: 29400321

Abstract:

Clostridium cellulovorans produces multi-enzyme complexes called cellulosomes capable of efficiently degrading cellulosic biomass. There are three xylanase genes containing a sequence corresponding to a dockerin domain that are necessary for constructing cellulosomes in the genome. Among the xylanases encoded by these genes, xylanase B (XynB) contains a catalytic domain belonging to glycoside hydrolase family 10 and a carbohydrate-binding module (CBM) at the N-terminus, making it a member of CBM family 22. In this study, XynB was cloned, overexpressed, purified and crystallized. XynB was crystallized using the hanging-drop vapour-diffusion method in the presence of 0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl pH 8.5, 32%(w/v) PEG 4000 at 293 K. X-ray diffraction analysis revealed that the crystal diffracted to 1.95 Å resolution and belonged to space group P212121, with unit-cell parameters a = 74.28, b = 77.55, c = 88.20 Å, α = β = γ = 90°. The data-evaluation statistics revealed high quality of the collected data, thereby establishing a solid basis for determination of the structure of cellulosomal xylanase from C. cellulovorans.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP6131904	Sodium acetate trihydrate		6131-90-4	Price

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