Characterization of a monoclinic crystal form of an enzyme of steroid metabolism, Δ5-3-ketosteroid isomerase

Edwin M Westbrook; Paul B Sigler; Helen Berman; Jenny P Glusker; Gerard Bunick; Ann Benson; Paul Talalay

doi:10.1016/0022-2836(76)90225-4

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Characterization of a monoclinic crystal form of an enzyme of steroid metabolism, Δ5-3-ketosteroid isomerase

Journal article

Peer reviewed

Characterization of a monoclinic crystal form of an enzyme of steroid metabolism, Δ5-3-ketosteroid isomerase

Edwin M Westbrook, Paul B Sigler, Helen Berman, Jenny P Glusker, Gerard Bunick, Ann Benson and Paul Talalay

Journal of molecular biology, Vol.103(3), pp.665-667

1976

DOI: https://doi.org/10.1016/0022-2836(76)90225-4

Abstract

A monoclinic crystal form ( P2 1, a = 140.4 A ̊ , b = 85.0 A ̊ , c = 94.5 A ̊ , β= 130.1 °) of Δ 5-3-ketosteroid isomerase from Pseudomonas testosteroni (EC 5.3.3.1), grown at pH 7.0, has been characterized. Crystal-density measurements show that the asymmetric unit contains 12 protomers ( M r = 13,394).

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Details

Title: Characterization of a monoclinic crystal form of an enzyme of steroid metabolism, Δ5-3-ketosteroid isomerase
Creators: Edwin M Westbrook
Paul B Sigler
Helen Berman
Jenny P Glusker
Gerard Bunick - Department of Chemistry University of Pennsylvania Philadelphia, Penn. 19174, U.S.A
Ann Benson
Paul Talalay
Publication Details: Journal of molecular biology, Vol.103(3), pp.665-667
Date published: 1976
Publisher: Elsevier Ltd
Academic Unit: Chemistry and Chemical Biology (SAS)
Language: English
Resource Type: Journal article
Identifiers: 991031665343504646