Crystallization and preliminary X-ray diffraction analysis of a protease inhibitor from the haemolymph of the Indian tasar silkworm Antheraea mylitta.
A protein with inhibitory activity against fungal proteases was purified from the haemolymph of the Indian tasar silkworm Antheraea mylitta and was crystallized using the hanging-drop vapour-diffusion method. Polyethylene glycol 3350 was used as a precipitant. Crystals belonged to space group P6(3)22, with unit-cell parameters a = b = 60.6, c = 85.1 angstroms. X-ray diffraction data were collected and processed to a maximum resolution of 2.1 angstroms.
Roy
Sobhan
S
Department of Biotechnology, Indian Institute of Technology, Kharagpur, India.
Aravind
Penmatsa
P
Madhurantakam
Chaithanya
C
Ghosh
Ananta Kumar
AK
Sankaranarayanan
Rajan
R
Das
Amit Kumar
AK
D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D003460:Crystallization; D005656:Fungal Proteins / Q000037:antagonists & inhibitors; D006458:Hemolymph / Q000201:enzymology*; D011480:Protease Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D014961:X-Ray Diffraction
D005656:Fungal Proteins; D011480:Protease Inhibitors