Crystallization and preliminary X-ray diffraction analysis of a plant ribonuclease from the seeds of the bitter gourd Momordica charantia.
Single crystals of ribonuclease Mc, a new class of plant ribonuclease from the seeds of the bitter gourd, were obtained from solutions of polyethylene glycol 8000 by the hanging-drop vapour diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 67.28 A, b = 75.21 A, c = 38.54 A. The assumption of one monomer per asymmetric unit gives rise to a Vm value of 2.29 A3/Da. The crystals diffract beyond 2.0 A resolution and are suitable for high resolution X-ray structure analysis.
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Protein Structure Laboratory, Imperial Cancer Research Fund, London, U.K.
Funatsu
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D003460:Crystallization; D010945:Plants, Edible / Q000201:enzymology*; D012260:Ribonucleases / Q000737:chemistry*; D014961:X-Ray Diffraction
D012260:Ribonucleases