Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/14746
Title: Crystallization and preliminary X-ray study of alkaline mannanase from an alkaliphilic Bacillus isolate
Authors: Akita, M
Takeda, N
Hirasawa, K
Hatada, Y
Ito, S
Horikoshi, K
Sakai, H
Kawamoto, M
Yamamoto, M
Grant, WD
First Published: Aug-2004
Publisher: International Union of Crystallography
Citation: ACTA CRYSTALLOGRAPHICA SECTION D: BIOLOGICAL CRYSTALLOGRAPHY, 2004, 60 (8), pp. 1490-1492
Abstract: An alkaline mannanase (EC 3.2.1.78) from the alkaliphilic Bacillus sp. strain JAMB-602 was cloned and sequenced. The deduced amino-acid sequence of the enzyme suggested that the enzyme consists of a catalytic and unknown additional domains. The recombinant enzyme expressed by B. subtilis was crystallized using the hanging-drop vapour-diffusion method at 277 K. X-ray diffraction data were collected to 1.65 Å. The crystal belongs to space group P2[subscript: 1]2[subscript: 1]2[subscript: 1], with unit-cell parameters a = 70.7, b = 79.5, c = 80.4 Å. The asymmetric unit contains one protein molecule, with a corresponding V[subscript: M] of 2.26 Å[superscript: 3] Da[superscript: -1] and a solvent content of 45.6%. Molecular replacement for initial phasing was carried out using the three-dimensional structure of a mannanase from Thermomonospora fusca as a search model, which corresponds to the catalytic domain of the alkaline mannanase. It gave sufficient phases to build the unknown domain.
DOI Link: 10.1107/S0907444904014313
ISSN: 0907-4449
Links: http://hdl.handle.net/2381/14746
http://scripts.iucr.org/cgi-bin/paper?S0907444904014313
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2004 International Union of Crystallography. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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