Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777

Erina Yoshida; Masafumi Hidaka; Shinya Fushinobu; Takashi Koyanagi; Hiromichi Minami; Hisanori Tamaki; Motomitsu Kitaoka; Takane Katayama; Hidehiko Kumagai

doi:10.1107/S1744309109042948

Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777

Erina Yoshida, Masafumi Hidaka, Shinya Fushinobu, Takashi Koyanagi, Hiromichi Minami, Hisanori Tamaki, Motomitsu Kitaoka, Takane Katayama, Hidehiko Kumagai

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

The intracellular β-glucosidase from Kluyveromyces marxianus NBRC1777 (KmBglI) belongs to glycoside hydrolase family 3 and has a unique domain architecture. Selenomethionine-labelled KmBglI was purified and crystallized by the hanging-drop vapour-diffusion method using the purified enzyme at 30 mg ml^-1, 0.04 M potassium dihydrogen phosphate pH 5.1, 16%(w/v) PEG 8000 and 20%(v/v) glycerol. The crystal belonged to space group C2, with unit-cell parameters a = 245.8, b = 148.7, c = 119.9 Å, β = 112.9°. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 Å resolution. A tetramer was assumed to be present in the asymmetric unit, which gave a Matthews coefficient of 2.6 Å³ Da^-1.

Original language	English
Pages (from-to)	1190-1192
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	65
Issue number	11
DOIs	https://doi.org/10.1107/S1744309109042948
Publication status	Published - 2009
Externally published	Yes

Keywords

Glycoside hydrolase family 3
Kluyveromyces marxianus NBRC1777
β-glucosidases

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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Yoshida, E., Hidaka, M., Fushinobu, S., Koyanagi, T., Minami, H., Tamaki, H., Kitaoka, M., Katayama, T., & Kumagai, H. (2009). Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(11), 1190-1192. https://doi.org/10.1107/S1744309109042948

Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777. / Yoshida, Erina; Hidaka, Masafumi; Fushinobu, Shinya et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 11, 2009, p. 1190-1192.

Research output: Contribution to journal › Article › peer-review

Yoshida, E, Hidaka, M, Fushinobu, S, Koyanagi, T, Minami, H, Tamaki, H, Kitaoka, M, Katayama, T & Kumagai, H 2009, 'Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 65, no. 11, pp. 1190-1192. https://doi.org/10.1107/S1744309109042948

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abstract = "The intracellular β-glucosidase from Kluyveromyces marxianus NBRC1777 (KmBglI) belongs to glycoside hydrolase family 3 and has a unique domain architecture. Selenomethionine-labelled KmBglI was purified and crystallized by the hanging-drop vapour-diffusion method using the purified enzyme at 30 mg ml-1, 0.04 M potassium dihydrogen phosphate pH 5.1, 16%(w/v) PEG 8000 and 20%(v/v) glycerol. The crystal belonged to space group C2, with unit-cell parameters a = 245.8, b = 148.7, c = 119.9 {\AA}, β = 112.9°. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 {\AA} resolution. A tetramer was assumed to be present in the asymmetric unit, which gave a Matthews coefficient of 2.6 {\AA}3 Da-1.",

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author = "Erina Yoshida and Masafumi Hidaka and Shinya Fushinobu and Takashi Koyanagi and Hiromichi Minami and Hisanori Tamaki and Motomitsu Kitaoka and Takane Katayama and Hidehiko Kumagai",

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AU - Fushinobu, Shinya

AU - Koyanagi, Takashi

AU - Minami, Hiromichi

AU - Tamaki, Hisanori

AU - Kitaoka, Motomitsu

AU - Katayama, Takane

AU - Kumagai, Hidehiko

PY - 2009

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N2 - The intracellular β-glucosidase from Kluyveromyces marxianus NBRC1777 (KmBglI) belongs to glycoside hydrolase family 3 and has a unique domain architecture. Selenomethionine-labelled KmBglI was purified and crystallized by the hanging-drop vapour-diffusion method using the purified enzyme at 30 mg ml-1, 0.04 M potassium dihydrogen phosphate pH 5.1, 16%(w/v) PEG 8000 and 20%(v/v) glycerol. The crystal belonged to space group C2, with unit-cell parameters a = 245.8, b = 148.7, c = 119.9 Å, β = 112.9°. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 Å resolution. A tetramer was assumed to be present in the asymmetric unit, which gave a Matthews coefficient of 2.6 Å3 Da-1.

AB - The intracellular β-glucosidase from Kluyveromyces marxianus NBRC1777 (KmBglI) belongs to glycoside hydrolase family 3 and has a unique domain architecture. Selenomethionine-labelled KmBglI was purified and crystallized by the hanging-drop vapour-diffusion method using the purified enzyme at 30 mg ml-1, 0.04 M potassium dihydrogen phosphate pH 5.1, 16%(w/v) PEG 8000 and 20%(v/v) glycerol. The crystal belonged to space group C2, with unit-cell parameters a = 245.8, b = 148.7, c = 119.9 Å, β = 112.9°. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 Å resolution. A tetramer was assumed to be present in the asymmetric unit, which gave a Matthews coefficient of 2.6 Å3 Da-1.

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Purification, crystallization and preliminary X-ray analysis of β-glucosidase from Kluyveromyces marxianus NBRC1777

Abstract

Keywords

ASJC Scopus subject areas

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