Abstract
Nicotiana alata S(F11)-RNase is an S-glycoprotein associated with gametophytic self-incompatibility. Crystals of S(F11)-RNase have been grown at room temperature using polyethylene glycol as a precipitant. A crystal diffracted to better than 1.4 A resolution at 100 K at the SPring-8 synchrotron-radiation source, indicating that it is very suitable for high-resolution structure analysis. The crystal belongs to the space group P2(1), with unit-cell parameters a = 65.86 (11), b = 44.73 (5), c = 64.36 (7) A, beta = 90.27 (9) degrees. The asymmetric unit contains two monomers, giving a crystal volume per protein mass (V(M)) of 2.05 A(3) Da(-1) and a solvent content of 39.6% by volume. A full set of X-ray diffraction data was collected to 1.55 A resolution with a completeness of 97.4%. A heavy-atom derivative has been successfully prepared with ethylmercury thiosalicylate (EMTS) and structure analysis is in progress.
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Schedule a callMore From: Acta crystallographica. Section D, Biological crystallography
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