Crystallographic study of the maize cytokinin glucoside-specific beta-glucosidase Zm-p60.1
| Authors | |
|---|---|
| Year of publication | 2000 |
| Type | Article in Proceedings |
| Conference | 19-th European Crystallographic Meeting - Abstracts book |
| MU Faculty or unit | |
| 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. |
| Related projects: |