Crystallization and preliminary X-ray characterization of aminopeptidase N fromEscherichia coli
- 26 June 2006
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 62 (7) , 699-701
- https://doi.org/10.1107/s1744309106021567
Abstract
A recombinant form of aminopeptidase N (molecular weight 99 kDa) from Escherichia coli was crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitating agent. The crystals belong to the hexagonal space group P3(1)21, with unit-cell parameters a = b = 120.5, c = 171.0 angstroms. The crystals are most likely to contain one molecule in the asymmetric unit, with a V(M) value of 3.62 angstroms3 Da(-1). Diffraction data were collected to 2.0 angstroms resolution using Cu Kalpha radiation from a rotating-anode X-ray generator.Keywords
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