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Purification, crystallization and preliminary X‐ray crystallographic analysis of glycosyltransferase‐1 from Bacillus cereus
Author(s) -
Hsieh YinCheng,
Chiu HsiHo,
Huang YenChieh,
Fun HoongKun,
Lu ChiaYu,
Li YawKuen,
Chen ChunJung
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14014629
Subject(s) - glycosyltransferase , cereus , bacillus cereus , crystallization , chemistry , crystallography , molecule , bacteria , biochemistry , stereochemistry , biology , organic chemistry , enzyme , genetics
Glycosyltransferases (GTs), which are distributed widely in various organisms, including bacteria, fungi, plants and animals, play a role in synthesizing biological compounds. Glycosyltransferase‐1 from Bacillus cereus ( Bc GT‐1), which is capable of transferring glucose to small molecules such as kaempferol and quercetin, has been identified as a member of the family 1 glycosyltransferases which utilize uridine diphosphate glucose (UDP‐glucose) as the sugar donor. Bc GT‐1 (molecular mass 45.5 kDa) has been overexpressed, purified and crystallized using the hanging‐drop vapour‐diffusion method. According to X‐ray diffraction of Bc GT‐1 crystals to 2.10 Å resolution, the crystal belonged to space group P 1, with unit‐cell parameters a = 54.56, b = 84.81, c = 100.12 Å, α = 78.36, β = 84.66, γ = 84.84°. Preliminary analysis indicates the presence of four Bc GT‐1 molecules in the asymmetric unit with a solvent content of 50.27%.