Crystallographic study of the maize cytokinin glucoside-specific beta-glucosidase Zm-p60.1

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Authors

MAREK Jaromír VÉVODOVÁ Jitka SU X.-D. ZOUHAR Jan BRZOBOHATÝ Břetislav

Year of publication 2000
Type Article in Proceedings
Conference 19-th European Crystallographic Meeting - Abstracts book
MU Faculty or unit

Faculty of Science

Citation
Field Genetics and molecular biology
Description Zm-p60.1, a cytokinin-glucoside-specific b-glucosidase from maize, is a key enzyme involved in plant development and growth. It has been over-expressed in soluble form from Escherichia coli with a His tag at its N-terminus, the recombinant protein has been purified and crystallized at room temperature using PEG 4000 as main precipitant. A flash-annealed monoclinic crystal diffracted to high resolution (beyond 2 A) with space group P21, and unit-cell parameters a = 55.66 A, b = 110.72 A, c = 72.94 A, b = 92.10 deg. Resulting crystal structure was solved by molecular replacement.
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