| Title : Crystallization and preliminary X-ray diffraction studies of mandelonitrile lyase from almonds - Lauble_1994_Proteins_19_343 |
| Author(s) : Lauble H , Muller K , Schindelin H , Forster S , Effenberger F |
| Ref : Proteins , 19 :343 , 1994 |
|
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. |
| PubMedSearch : Lauble_1994_Proteins_19_343 |
| PubMedID: 7984630 |
Lauble H, Muller K, Schindelin H, Forster S, Effenberger F (1994)
Crystallization and preliminary X-ray diffraction studies of mandelonitrile lyase from almonds
Proteins
19 :343
Lauble H, Muller K, Schindelin H, Forster S, Effenberger F (1994)
Proteins
19 :343