Crystallization and preliminary X-ray study of saporin, a ribosome-inactivating protein from Saponaria officinalis.
Single crystals of the protein saporin isolated from the seeds of S. officinalis have been grown by the vapor-diffusion method using ammonium sulfate as precipitant. The crystals are tetragonal, space group P4122 (P4322), with cell dimensions a = b = 67.53 and c = 119. 67 A, and diffract to 2.0 A resolution on a rotating-anode X-ray source. The asymmetric unit contains one molecule, corresponding to a volume of the asymmetric unit per unit mass (Vm) of 2.38 A3 Da-1.
Department of Biochemical Sciences and CNR, Centre for Molecular Biology, Università di Roma 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy. savino@biosig.phys.uniromal.it
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Savino
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Federici
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Brancaccio
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Ippoliti
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Lendaro
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Tsernoglou
D003460:Crystallization; D018360:Crystallography, X-Ray; D000922:Immunotoxins; D009699:N-Glycosyl Hydrolases; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D054789:Ribosome Inactivating Proteins, Type 1; D000076985:Saporins
D000922:Immunotoxins; D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; D009699:N-Glycosyl Hydrolases; D000076985:Saporins