Premium
Crystallization and preliminary X‐ray diffraction studies of mandelonitrile lyase from almonds
Author(s) -
Lauble Hanspeter,
Müller Kirsten,
Schindelin Hermann,
Förster Siegfried,
Effenberger Franz
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340190410
Subject(s) - monoclinic crystal system , lyase , crystallization , polyethylene glycol , chemistry , resolution (logic) , crystallography , enzyme , organic chemistry , crystal structure , artificial intelligence , computer science
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 l with unit cell parameters a = 69.9, b = 95.1, c = 95.6 Å, and β = 118.5°. A complete set of diffraction data has been collected to 2.6 Å resolution on native crystals of isoenzyme III. © 1994 Wiley‐Liss, Inc.