PMID:10739936
| Citation |
Kozak, M and Jaskólski, M (2000) Crystallization and preliminary crystallographic studies of a new crystal form of Escherichia coli L--asparaginase II (Ser58Ala mutant). Acta Crystallogr. D Biol. Crystallogr. 56:509-11 |
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| Abstract |
Periplasmic Escherichia coli L-asparaginase II with an Ser58Ala mutation in the active-site cavity has been crystallized in a new orthorhombic form (space group P2(1)2(1)2). Crystals of this polymorph suitable for X-ray diffraction have been obtained by vapour diffusion using two sets of conditions: (i) 1% agarose gel using MPD as precipitant (pH 4.8) and (ii) liquid droplets using PEG-MME 550 (pH 9.0). The crystals grown in agarose gel are characterized by unit-cell parameters a = 226.9, b = 128.4, c = 61.9 A and diffract to 2.3 A resolution. The asymmetric unit contains six protein molecules arranged into one pseudo-222-symmetric homotetramer and an active-site competent dimer from which another homotetramer is generated by crystallographic symmetry. |
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| Keywords |
Alanine; Amino Acid Substitution; Asparaginase/chemistry; Asparaginase/isolation & purification; Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Serine |
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