Preliminary crystallographic data for protease omega.
Protease omega from Carica papaya L. has been purified and crystallized. The crystals are trigonal, space group P3(1)12 (or P3(2)12), with a = 7.42 +/- 0.02 nm, c = 7.79 +/- 0.02 nm with one molecule in the asymmetric unit. The crystals diffract to 0.19-nm resolution using synchrotron radiation.
Department of Biotechnology and Enzymology, Reading Laboratory, Shinfield, England.
R W
RW
Pickersgill
I G
IG
Sumner
P W
PW
Goodenough
D003461:Crystallography; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification; D005638:Fruit / Q000201:enzymology; D010206:Papain; D011487:Protein Conformation; D014961:X-Ray Diffraction
D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C018745:actinidain; D010206:Papain