Purification, crystallisation and preliminary X-ray diffraction study of ribosome inactivating protein: saporin.
We report here the crysallisation and molecular replacement results on the structure determination of S-9 isoform of the ribosome inactivating protein saporin. The protein was purified to homogeneity by a simple and efficient protocol. The crystals belong to the space group I4l with a = b = 91.47 A, c = 150.66 A and contain two molecules in the asymmetric unit.
Kumar
M
M
Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai, India.
Dattagupta
S
S
Kannan
K K
KK
Hosur
M V
MV
D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D000922:Immunotoxins; D009699:N-Glycosyl Hydrolases; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D020033:Protein Isoforms / Q000302:isolation & purification; D054789:Ribosome Inactivating Proteins, Type 1; D000076985:Saporins; D014961:X-Ray Diffraction