Crystallization and preliminary X-ray study of saporin, a ribosome-inactivating protein from Saponaria officinalis.
Acta Crystallogr D Biol Crystallogr
; 54(Pt 4): 636-8, 1998 Jul 01.
Article
in En
| MEDLINE
| ID: mdl-9761860
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 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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Plant Proteins
/
Immunotoxins
/
N-Glycosyl Hydrolases
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
1998
Document type:
Article
Affiliation country:
Italy
Publication country:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA