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Crystallization and preliminary X‐ray crystallographic analysis of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T‐3040
Author(s) -
Suzuki Nobuhiro,
Kim YoungMin,
Momma Mitsuru,
Fujimoto Zui,
Kobayashi Mikihiko,
Kimura Atsuo,
Funane Kazumi
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911301991x
Subject(s) - bacillus circulans , crystallography , crystallization , molecule , resolution (logic) , intramolecular force , chemistry , escherichia coli , materials science , crystal structure , stereochemistry , organic chemistry , biochemistry , enzyme , artificial intelligence , computer science , gene
Bacillus circulans T‐3040 cycloisomaltooligosaccharide glucanotransferase (BcCITase) catalyses an intramolecular transglucosylation reaction and produces cycloisomaltooligosaccharides from dextran. BcCITase was overexpressed in Escherichia coli in two different forms and crystallized by the sitting‐drop vapour‐diffusion method. The crystal of BcCITase bearing an N‐terminal His 6 tag diffracted to a resolution of 2.3 Å and belonged to space group P 3 1 21, containing a single molecule in the asymmetric unit. The crystal of BcCITase bearing a C‐terminal His 6 tag diffracted to a resolution of 1.9 Å and belonged to space group P 2 1 2 1 2 1 , containing two molecules in the asymmetric unit.

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