Crystallization and preliminary crystallographic analysis of dextranase from Streptococcus mutans

Streptococcus mutans dextranase hydrolyzes the internal α‐1,6‐linkages of dextran and belongs to glycoside hydrolase family 66. An N‐ and C‐terminal deletion mutant of S. mutans dextranase was crystallized by the sitting‐drop vapour‐diffusion method. The crystals diffracted to a resolution of 1.6 Å...

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Published inActa crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 12; pp. 1542 - 1544
Main Authors Suzuki, Nobuhiro, Kim, Young-Min, Fujimoto, Zui, Momma, Mitsuru, Kang, Hee-Kwon, Funane, Kazumi, Okuyama, Masayuki, Mori, Haruhide, Kimura, Atsuo
Format Journal Article
LanguageEnglish
Published 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.12.2011
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Summary:Streptococcus mutans dextranase hydrolyzes the internal α‐1,6‐linkages of dextran and belongs to glycoside hydrolase family 66. An N‐ and C‐terminal deletion mutant of S. mutans dextranase was crystallized by the sitting‐drop vapour‐diffusion method. The crystals diffracted to a resolution of 1.6 Å and belonged to space group P21, with unit‐cell parameters a = 53.2, b = 89.7, c = 63.3 Å, β = 102.3°. Assuming that the asymmetric unit of the crystal contained one molecule, the Matthews coefficient was calculated to be 4.07 Å3 Da−1; assuming the presence of two molecules in the asymmetric unit it was calculated to be 2.03 Å3 Da−1.
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These authors contributed equally to this work.
Present address: Eco-Friendly Biomaterial Research Center and AI Control Material Research Center, Korea Research Institute of Bioscience and Biotechnology, 181 Ipsin-gil, Jeongeup-si, Jeonbuk 580-185, Republic of Korea.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309111038425