Crystallization and preliminary X-ray study of γ-­type cyclodextrin glycosyltransferase from Bacillus clarkii

A γ‐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 Å. The crystal belongs to space group R3, with unit‐cell parameters a = b = 211.6, c = 52.7 Å. The asymmetri...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-03, Vol.60 (3), p.586-587
Hauptverfasser: Akita, Masatake, Hatada, Yuji, Hidaka, Yuko, Ohta, Yukari, Takada, Masayasu, Nakagawa, Yoshinori, Ogawa, Koichi, Nakakuki, Teruo, Ito, Susumu, Horikoshi, Koki
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Sprache:eng
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Zusammenfassung:A γ‐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 Å. The crystal belongs to space group R3, with unit‐cell parameters a = b = 211.6, c = 52.7 Å. The asymmetric unit contains one protein molecule, with a corresponding VM of 3.03 Å3 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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444904001076