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;Brancaccio A;
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).File in questo prodotto:
| File | Dimensione | Formato | |
|---|---|---|---|
|
prod_244295-doc_64067.pdf
solo utenti autorizzati
Descrizione: Crystallization and preliminary X-ray study of saporin, a ribosome-inactivating protein from Saponaria officinalis
Dimensione
171.83 kB
Formato
Adobe PDF
|
171.83 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
