Crystallization and preliminary X-ray studies of an aspartate aminotransferase mutant from Escherichia coli

Crystallization and preliminary X-ray studies of an aspartate aminotransferase mutant from Escherichia coli

Mutant aspartate aminotransferase V39L (Val39 replaced by Leu) from Escherichia coli has been crystallized into a monoclinic cell from a polyethylene glycol solution (pH 7.5) by vapor diffusion. The space group and the unit cell dimensions have been determined using a precession camera, a CAD4 diffr...

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Veröffentlicht in:Journal of molecular biology 1989-10, Vol.209 (3), p.499-501
Hauptverfasser: Jäger, J., Köhler, E., Tucker, P., Sauder, U., Housley-Markovic, Z., Fotheringham, I., Edwards, M., Hunter, M., Kirschner, K., Jansonius, J.N.
Format: Artikel
Sprache:eng
Schlagworte:
Aspartate Aminotransferases
Biological and medical sciences
Crystalline structure
Crystallization
Escherichia coli - enzymology
Fundamental and applied biological sciences. Psychology
leucine
Models, Molecular
Molecular biophysics
Mutation
Protein Conformation
Structure in molecular biology
valine
X-Ray Diffraction
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Zusammenfassung:Mutant aspartate aminotransferase V39L (Val39 replaced by Leu) from Escherichia coli has been crystallized into a monoclinic cell from a polyethylene glycol solution (pH 7.5) by vapor diffusion. The space group and the unit cell dimensions have been determined using a precession camera, a CAD4 diffractometer and a Nicolet Xentronics area detector to be P2 1 with a = 86.8 A ̊ , b = 79.9 A ̊ , c = 89.4 A ̊ , β = 118.74 °. The crystals diffract to better than 2.3 Å and are suitable for X-ray structure analysis.
ISSN:0022-2836
1089-8638
DOI:10.1016/0022-2836(89)90014-4