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Crystallization and preliminary X-ray diffraction studies of mandelonitrile lyase from almonds.

作者信息

Lauble H, Müller K, Schindelin H, Förster S, Effenberger F

机构信息

Institut für Organische Chemie und Isotopenforschung, Universität Stuttgart, Germany.

出版信息

Proteins. 1994 Aug;19(4):343-7. doi: 10.1002/prot.340190410.

DOI:10.1002/prot.340190410
PMID:7984630
Abstract

Single crystals of three different isoenzymes of (R)-(+) mandelonitrile lyase (hydroxynitrile lyase) from almonds (Prunus amygdalus) have been obtained by hanging drop vapor diffusion using polyethylene glycol 4000 and isopropanol as co-precipitants. The crystals belong to the monoclinic space group P2(1) with unit cell parameters a = 69.9, b = 95.1, c = 95.6 A, and beta = 118.5 degrees. A complete set of diffraction data has been collected to 2.6 A resolution on native crystals of isoenzyme III.

摘要

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