Preliminary crystallographic data on the complex of bovine alpha-chymotrypsin with the recombinant proteinase inhibitor eglin c from Hirudo medicinalis.
The molecular complex built by bovine alpha-chymotrypsin and the recombinant proteinase inhibitor eglin c from Hirudo medicinalis has been crystallized from polyethylene glycol solutions, using a twofold molar excess of the inhibitor with respect to the serine proteinase. The optimum pH for crystal growth is 6.5. The crystals belong to the monoclinic space group P2(1), with unit cell constant: a = 55.3 A, b = 59.4 A, c = 42.5 A, beta = 99.0 degrees; one complex moiety is present per asymmetric unit. The crystals diffract to 2.0 A resolution and are suitable for detailed X-ray crystallographic investigations.
Pugliese
L
L
Dipartimento di Genetica e Microbiologia, Università di Pavia, Italy.
Gatti
G
G
Bolognesi
M
M
Coda
A
A
Menegatti
E
E
Schnebli
H P
HP
Ascenzi
P
P
Amiconi
G
G
D000818:Animals; D002417:Cattle; D002918:Chymotrypsin; D007865:Leeches; D046911:Macromolecular Substances; D011480:Protease Inhibitors; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011480:Protease Inhibitors; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins; C028656:eglin proteinase inhibitors; D002918:Chymotrypsin