Purification, Crystallization and Preliminary X-ray Analysis of a Maize Cytokinin-glucoside-specific b-Glucosidase.
| Authors | |
|---|---|
| Year of publication | 2001 |
| Type | Article in Periodical |
| Magazine / Source | Acta Crystallogr., Sect.D |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | beta-glucosidase; hydrolase; protein crystallography |
| Description | Zm-p60.1, a cytokinin-glucoside-specific beta-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 few forms of crystals have been observed from very similar conditions. 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. The asymmetric unit is estimated and confirmed by molecular replacement solution to contain a Zm-p60.1 dimer, giving a crystal volume per protein mass (Vm) of 1.89 A3 Da-1 and a solvent content of 35%. |
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