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Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40

Lee, Saeyoung and Lee, Jonas Yun and Ha, Sung Chul and Jung, Jina and Shin, Dong Hae and Kim, Kyoung Heon and Choi, In-Geol (2009) Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 65 (12). pp. 1299-1301. ISSN 1744-3091. PMCID PMC2802886.

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Many agarolytic bacteria degrade agar polysaccharide into the disaccharide unit neoagarobiose [O-3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose] using various β-agarases. Neoagarobiose hydrolase is an enzyme that acts on the α-1,3 linkage in neoagarobiose to yield D-galactose and 3,6-anhydro-L-galactose. This activity is essential in both the metabolism of agar by agarolytic bacteria and the production of fermentable sugars from agar biomass for bioenergy production. Neoagarobiose hydrolase from the marine bacterium Saccharophagus degradans 2-40 was overexpressed in Escherichia coli and crystallized in the monoclinic space group C2, with unit-cell parameters a = 129.83, b = 76.81, c = 90.11 Å, β = 101.86°. The crystals diffracted to 1.98 Å resolution and possibly contains two molecules in the asymmetric unit.

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Additional Information:© 2009 International Union of Crystallography. Received 1 September 2009. Accepted 2 November 2009. We are grateful to Professor Sung-Hou Kim for letting us use his facility for protein purification and crystallization, to Dr Jose Henrique Pereira for his help and advice in preparing this manuscript and to the staff of the Berkeley Center for Structural Biology for their help and advice. The Advance Light Source at Lawrence Berkeley National Laboratory is supported by the Director, Office of Science, Office of Basic Energy Sciences, Materials Sciences Division of the US Department of Energy under Contract No. DE-AC03-76SF00098.
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Department of Energy (DOE)DE-AC03-76SF00098
Subject Keywords:bioenergy; neoagarobiose; hydrolases.
Issue or Number:12
PubMed Central ID:PMC2802886
Record Number:CaltechAUTHORS:20100111-102113543
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:17133
Deposited By: Tony Diaz
Deposited On:12 Jan 2010 22:17
Last Modified:21 May 2020 22:29

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