Preliminary crystallographic data on the complex of bovine α-chymotrypsin with the recombinant proteinase inhibitor eglin c from Hirudo medicinalis

Luisa Pugliese, Giuseppina Gatti, Martino Bolognesi, Alessandro Coda, Enea Menegatti, Hans Peter Schnebli, Paolo Ascenzi, Gino Amiconi

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)511-513
Number of pages3
JournalJournal of Molecular Biology
Volume208
Issue number3
DOIs
Publication statusPublished - Aug 5 1989

ASJC Scopus subject areas

  • Virology

Fingerprint Dive into the research topics of 'Preliminary crystallographic data on the complex of bovine α-chymotrypsin with the recombinant proteinase inhibitor eglin c from Hirudo medicinalis'. Together they form a unique fingerprint.

Cite this