Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.

Published: July 2006

AI Article Synopsis

  • A recombinant aminopeptidase N from E. coli was successfully crystallized using the hanging-drop vapor-diffusion method with ammonium sulfate as a precipitant.
  • The resulting crystals are classified in the hexagonal space group P3(1)21, with specific unit-cell dimensions of a = b = 120.5 angstroms and c = 171.0 angstroms.
  • Diffraction data for the crystals were acquired up to a resolution of 2.0 angstroms using Cu Kalpha radiation from a rotating-anode X-ray generator.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242940PMC
http://dx.doi.org/10.1107/S1744309106021567DOI Listing

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