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 P4(1)22 (P4(3)22), with cell-dimensions a = b = 67.53 and c = 119.67 Angstrom, and diffract to 2.0 Angstrom 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 (V-m) of 2.38 Angstrom(3) Da(-1).
Crystallization and preliminary X-ray study of Saporin, a Ribosome Inactivating Protein from Saponaria officinalis / Savino, C; Federici, L; Brancaccio, A; Ippoliti, R; Lendaro, Eugenio; Tsernoglou, Demetrius. - In: ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY. - ISSN 0907-4449. - ELETTRONICO. - D54:(1998), pp. 636-638. [10.1107/S0907444997012249]
Crystallization and preliminary X-ray study of Saporin, a Ribosome Inactivating Protein from Saponaria officinalis
LENDARO, Eugenio;TSERNOGLOU, Demetrius
1998
Abstract
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 P4(1)22 (P4(3)22), with cell-dimensions a = b = 67.53 and c = 119.67 Angstrom, and diffract to 2.0 Angstrom 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 (V-m) of 2.38 Angstrom(3) Da(-1).I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
