Crystallographic study of an esteroproteolytic enzyme

L. M. Amzel, H. P. Avey, L. N. Becka, R. J. Poljak

Research output: Contribution to journalArticlepeer-review


The esteroproteolytic enzyme, a serine protease from porcine pancreas, has been crystallized and characterized by X-ray diffraction. Two closely related crystal forms were observed. The unit cell dimensions of the first form are a = 59.2 A ̊, b = 96.4 A ̊ and c = 47.4 A ̊, space group P21212 with one molecule (mol. wt 30,000) per asymmetric unit. The unit cell dimensions of the second form are a = 59.2 A ̊, b = 96.4 A ̊ and c = 94.8 A ̊, space group P212121. Mercury derivatives of enzyme inhibitors were used to obtain multiple isomorphous heavy-atom substituents suitable for phase determination.

Original languageEnglish (US)
Pages (from-to)87-89
Number of pages3
JournalJournal of molecular biology
Issue number1
StatePublished - Nov 25 1973

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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