Back to Search Start Over

Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome.

Authors :
Borek, Dominika
Jaskóiski, Mariusz
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.

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