Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin

Dong Hae Shin, Kwang Yeon Hwang, Kyeong Kyu Kim, Hae Ryun Lee, Cheol Soon Lee, Chin Ha Chung, Se Won Suh

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


Ecotin, a novel serine protease inhibitor isolated from Escherichia coli, has been crystallized using polyethylene glycol 1500 as the precipitating agent. The crystals belong to the orthorhombic space group P212121, with unit cell parameters of a = 39.22 Å, b = 84.86 Å, and c = 98.74 Å. The asymmetric unit contains one dimeric molecule of ecotin, with a crystal volume per protein mass (Vm) of 2.55 Å3/Da and a solvent content of 51.8% by volume. The crystals diffract to at least 2.2 Å using a conventional X-ray source, and X-ray data have been collected to 2.7 Å Bragg spacing from a native crystal.

Original languageEnglish
Pages (from-to)1157-1158
Number of pages2
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - 1993 Feb 20
Externally publishedYes


  • Crystallization
  • Ecotin
  • Preliminary X-ray analysis
  • Serine protease inhibitor
  • X-ray crystallography

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Structural Biology


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