Crystallization and preliminary X-ray study of gamma-type cyclodextrin glycosyltransferase from Bacillus clarkii.
A gamma-cyclodextrin glycosyltransferase (EC 2.4.1.19) from Bacillus clarkii was crystallized using the hanging-drop vapour-diffusion method at 293 K. X-ray diffraction data were collected to 2.2 A. The crystal belongs to space group R3, with unit-cell parameters a = b = 211.6, c = 52.7 A. The asymmetric unit contains one protein molecule, with a corresponding V(M) of 3.03 A(3) Da(-1) and a solvent content of 59.4%. Molecular replacement was successfully carried out using a homology model based on the three-dimensional structure of the CGTase from Thermonanaerobacterium thermosulfurigenes EM1 as a search model.
Akita
Masatake
M
Japan Marine Science and Technology Center, 2-15 Natsushima, Yokosuka 237-0061, Japan. akitam@jamstec.go.jp
Hatada
Yuji
Y
Hidaka
Yuko
Y
Ohta
Yukari
Y
Takada
Masayasu
M
Nakagawa
Yoshinori
Y
Ogawa
Koichi
K
Nakakuki
Teruo
T
Ito
Susumu
S
Horikoshi
Koki
K
D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005964:Glucosyltransferases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D040681:Structural Homology, Protein
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D005964:Glucosyltransferases; C019963:cyclomaltodextrin glucanotransferase