Acta Crystallographica Section D

Biological Crystallography

Volume 57, Part 1 (January 2001)

crystallization papers

Acta Cryst. (2001). D57, 140-142 [ doi:10.1107/S0907444900014001 ]

Purification, crystallization and preliminary X-ray analysis of a maize cytokinin glucoside specific -glucosidase

J. Vévodová, J. Marek, J. Zouhar, B. Brzobohatý and X.-D. Su

Abstract: Zm-p60.1, a cytokinin glucoside specific [beta] -glucosidase from maize, is a key enzyme involved in plant development and growth. It has been overexpressed 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 the main precipitant. At least three crystal forms have been observed from very similar growth conditions. A flash-annealed monoclinic crystal diffracted to high resolution (beyond 2 Å) with space group P2₁ and unit-cell parameters a = 55.66, b = 110.72, c = 72.94 Å, [beta] = 92.10°. The asymmetric unit is estimated and confirmed by molecular-replacement solution to contain one Zm-p60.1 dimer, giving a crystal volume per protein mass (V_M) of 1.89 Å³ Da^-1 and a solvent content of 35%.

Keywords: -glucosidase; hydrolases.