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Crystallization and Preliminary X-ray Crystallographic Studies of Ribonuclease LE from Lycopersicon esculentum



The ribonuclease LE, a plant ribonuclease from lycopersicon esculentum, has been crystallized by the hanging-drop vapour diffusion method using polyethylene glycol 1,540 as the precipitating agent. The
crystals belong to an orthorhombic space group P2,2,2, with cell dimensions of a = 74.10 A, b = 78.72 A, and c
= 33.00 A. There is one molecule per asymmetric unit. The crystals diffract to at least 2.0 A resolution and
are suitable for X-ray structure analysis at high resolution.
