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Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome.
- Source :
- Acta Crystallographica: Section D (Wiley-Blackwell); Nov2000, Vol. 56 Issue 11, p1505-1507, 3p
- Publication Year :
- 2000
-
Abstract
- The article presents information on the crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome. l-Asparaginases (E.C. 3.5.1.1) are hydrolases which catalyze the breakdown of l-asparagine to l-aspartate. In the crystallization experiments it was found that addition of magnesium chloride was necessary for the formation of larger diffraction-quality crystals. Typical single crystals of EcAIII grown in the conditions described above have a prismatic habit but are nearly always malformed, i.e. they have voids or holes at one end of the prism.
- Subjects :
- ASPARAGINASE
ENTEROBACTERIACEAE
ESCHERICHIA coli
CRYSTALLIZATION
AMIDASES
GENOMES
Subjects
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 56
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 15005020
- Full Text :
- https://doi.org/10.1107/S0907444900010076