These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Crystallization and preliminary crystallographic analysis of dextranase from Streptococcus mutans. Author: Suzuki N, Kim YM, Fujimoto Z, Momma M, Kang HK, Funane K, Okuyama M, Mori H, Kimura A. Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2011 Dec 01; 67(Pt 12):1542-4. PubMed ID: 22139161. Abstract: 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 P2(1), 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 Å(3) Da(-1); assuming the presence of two molecules in the asymmetric unit it was calculated to be 2.03 Å(3) Da(-1).[Abstract] [Full Text] [Related] [New Search]