Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli

Citation
I. Polikarpov et al., Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli, ACT CRYST D, 55, 1999, pp. 1616-1617
Citations number
18
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
9
Pages
1616 - 1617
Database
ISI
SICI code
0907-4449(199909)55:<1616:PAPXDS>2.0.ZU;2-H
Abstract
L-Asparaginase is an enzyme which hydrolyzes asparagine to produce aspartic acid and ammonia. It is an effective chemotherapeutic drug, especially in the treatment of acute lymphoblastic leukaemia in children. The enzyme from Escherichia coli was crystallized in a new crystal form with space group C 2,unit-cell parameters a = 76.3 (0), b = 134.6(2), c = 64.8.(7) Angstrom, b eta = 110.5(1)degrees and a dimer in the asymmetric unit. Synchrotron-radia tion diffraction data have been collected to 1.95 Angstrom resolution.