Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein.
J Mol Biol
; 226(1): 281-3, 1992 Jul 05.
Article
en En
| MEDLINE
| ID: mdl-1619659
ABSTRACT
Mirabilis antiviral protein is a single-chain ribosome-inactivating protein purified from the tuberous root of Mirabilis jalapa L. We obtained several forms of crystals of the protein by the hanging drop vapor diffusion method, but most of these crystals were not suitable for X-ray crystallography. After refining the growth conditions, crystals of crystallographic quality were grown in 20-microliters droplets of an equi-volume mixture of 1.5% (w/v) protein solution and a reservoir solution containing 49 to 50% (w/v) ammonium sulfate and 50 mM-ammonium citrate (pH 5.4) at room temperature. Addition of 2 mM-adenine sulfate reduced twinning and "crystal shower". The resulting trigonal crystals diffract beyond 2.5 A resolution using a rotating anode X-ray generator. The space group was determined to be P3(1)21 or P3(2)21 (a = b = 103.9.A, c = 134.6 A, alpha = beta = 90 degrees, gamma = 120 degrees) based on their precession photography of h0l and hk0 zones. There seems to be three monomers in an asymmetric unit for VM = 2.51 A3/Da.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Antivirales
/
Proteínas de Plantas
/
Plantas
/
N-Glicosil Hidrolasas
Idioma:
En
Revista:
J Mol Biol
Año:
1992
Tipo del documento:
Article