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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 11(65), p. 1190-1192, 2009

DOI: 10.1107/s1744309109042948

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Purification, crystallization and preliminary X-ray analysis of β-glucosidase fromKluyveromyces marxianusNBRC1777

Journal article published in 2009 by Erina Yoshida, Masafumi Hidaka, Shinya Fushinobu ORCID, Takashi Koyanagi, Hiromichi Minami, Hisanori Tamaki, Motomitsu Kitaoka, Takane Katayama ORCID, Hidehiko Kumagai
This paper is available in a repository.
This paper is available in a repository.

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Abstract

The intracellular beta-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 unitcell parameters a = 245.8, b = 148.7, c = 119.9 angstrom, beta = 112.9 degrees. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 angstrom resolution. A tetramer was assumed to be present in the asymmetric unit, which gave a Matthews coefficient of 2.6 angstrom(3) Da(-1).