Crystallographic study of an esteroproteolytic enzyme

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

Research output: Contribution to journalArticle

Abstract

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
Volume81
Issue number1
DOIs
StatePublished - Nov 25 1973

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Serine Proteases
Enzyme Inhibitors
Enzymes
Mercury
X-Ray Diffraction
Pancreas
Swine

ASJC Scopus subject areas

  • Virology

Cite this

Crystallographic study of an esteroproteolytic enzyme. / Amzel, Mario L; Avey, H. P.; Becka, L. N.; Poljak, R. J.

In: Journal of Molecular Biology, Vol. 81, No. 1, 25.11.1973, p. 87-89.

Research output: Contribution to journalArticle

Amzel, Mario L ; Avey, H. P. ; Becka, L. N. ; Poljak, R. J. / Crystallographic study of an esteroproteolytic enzyme. In: Journal of Molecular Biology. 1973 ; Vol. 81, No. 1. pp. 87-89.
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