Volume 65, Issue 9 pp. 949-951

Purification, crystallization and preliminary X-ray analysis of urease from jack bean (Canavalia ensiformis)

Anuradha Balasubramanian

Anuradha Balasubramanian

Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India

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Karthe Ponnuraj

Karthe Ponnuraj

Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India

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First published: 21 September 2009
Citations: 2
Karthe Ponnuraj, e-mail: [email protected]

Abstract

Plant urease is a seed protein that is common in most legumes. It is also common in many bacteria and fungi and several species of yeast. Urease allows organisms to use exogenous and internally generated urea as a nitrogen source by catalyzing the hydrolysis of urea to ammonia and carbon dioxide. Urease from jack bean meal was purified to electrophoretic homogeneity using a series of steps involving acetone precipitation and size-exclusion and ion-exchange chromatography. The jack bean urease was crystallized and the resulting crystals diffracted to 2.05 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6322, with unit-cell parameters a = b = 138.57, c = 198.36 Å.

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