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 in | Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 12; pp. 1542 - 1544 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01.12.2011
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Subjects | |
Online Access | Get full text |
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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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Bibliography: | istex:6F2625F96B68298741E76262B1D9F94E6B87D1F7 ark:/67375/WNG-9MV7V1MZ-L ArticleID:AYF2PU5347 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 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 |