Abstract
The molecular complex built by bovine α-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 P21, with unit cell constant: a = 55.3 A ̊, b = 59.4 A ̊, c = 42.5 A ̊, β = 99.0 °; one complex moiety is present per asymmetric unit. The crystals diffract to 2.0 Å resolution and are suitable for detailed X-ray crystallographic investigations.
| Original language | English |
|---|---|
| Pages (from-to) | 511-513 |
| Number of pages | 3 |
| Journal | Journal of Molecular Biology |
| Volume | 208 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Aug 5 1989 |
Fingerprint
ASJC Scopus subject areas
- Virology
Cite this
Preliminary crystallographic data on the complex of bovine α-chymotrypsin with the recombinant proteinase inhibitor eglin c from Hirudo medicinalis. / Pugliese, Luisa; Gatti, Giuseppina; Bolognesi, Martino; Coda, Alessandro; Menegatti, Enea; Schnebli, Hans Peter; Ascenzi, Paolo; Amiconi, Gino.
In: Journal of Molecular Biology, Vol. 208, No. 3, 05.08.1989, p. 511-513.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Preliminary crystallographic data on the complex of bovine α-chymotrypsin with the recombinant proteinase inhibitor eglin c from Hirudo medicinalis
AU - Pugliese, Luisa
AU - Gatti, Giuseppina
AU - Bolognesi, Martino
AU - Coda, Alessandro
AU - Menegatti, Enea
AU - Schnebli, Hans Peter
AU - Ascenzi, Paolo
AU - Amiconi, Gino
PY - 1989/8/5
Y1 - 1989/8/5
N2 - The molecular complex built by bovine α-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 P21, with unit cell constant: a = 55.3 A ̊, b = 59.4 A ̊, c = 42.5 A ̊, β = 99.0 °; one complex moiety is present per asymmetric unit. The crystals diffract to 2.0 Å resolution and are suitable for detailed X-ray crystallographic investigations.
AB - The molecular complex built by bovine α-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 P21, with unit cell constant: a = 55.3 A ̊, b = 59.4 A ̊, c = 42.5 A ̊, β = 99.0 °; one complex moiety is present per asymmetric unit. The crystals diffract to 2.0 Å resolution and are suitable for detailed X-ray crystallographic investigations.
UR - http://www.scopus.com/inward/record.url?scp=0024962234&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024962234&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(89)90516-0
DO - 10.1016/0022-2836(89)90516-0
M3 - Article
C2 - 2795659
AN - SCOPUS:0024962234
VL - 208
SP - 511
EP - 513
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -