PMID:11752789
| Citation |
Kozak, M, Borek, D, Janowski, R and Jaskólski, M (2002) Crystallization and preliminary crystallographic studies of five crystal forms of Escherichia coli L-asparaginase II (Asp90Glu mutant). Acta Crystallogr. D Biol. Crystallogr. 58:130-2 |
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| Abstract |
L-Asparaginase II from Escherichia coli with an Asp90Glu mutation in the active site has been crystallized in five polymorphic forms. Crystals of all polymorphs suitable for X-ray diffraction experiments were obtained by the vapour-diffusion method. Crystals of form I belong to the monoclinic system (space group C2), have unit-cell parameters a = 73.1, b = 133.1, c = 62.6 A, beta = 108.8 degrees and diffract to 2.27 A resolution. Three of the crystal forms are orthorhombic, with unit-cell parameters a = 225.4, b = 128.0, c = 62.6 A (form II, P2(1)2(1)2), a = 59.9, b = 71.2, c = 130.6 A (form III, primitive cell) and a = 73.8, b = 122.1, c = 124.2 A (form IV, P2(1)2(1)2(1) or P2(1)2(1)2); the crystals diffract to 2.33, 3.5 and 1.7 A, respectively. Polymorph V is trigonal, space group P3(1)21, with unit-cell parameters a = 123.1, c = 83.8 A; the crystals diffract to 2.65 A resolution. |
| Links | |
| Keywords |
Asparaginase/chemistry; Asparaginase/genetics; Aspartic Acid/genetics; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Glutamic Acid/genetics; Mutation; Protein Conformation |
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