Skip to main content
padlock icon - secure page this page is secure

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

Buy Article:

$47.00 + tax (Refund Policy)

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 P3121, with unit‐cell parameters a = b = 120.5, c = 171.0 Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a V M value of 3.62 Å3 Da−1. Diffraction data were collected to 2.0 Å resolution using Cu Kα radiation from a rotating‐anode X‐ray generator.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: aminopeptidase N

Document Type: Research Article

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

Publication date: July 1, 2006

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more