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

Journal Article · Sat Jul 01 00:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106021567· OSTI ID:22360193

Onohara, Yuko; Nakajima, Yoshitaka; Ito, Kiyoshi; Xu, Yue; Nakashima, Kanako; Ito, Takashi; Yoshimoto, Tadashi ^[1]

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

E. coli aminopeptidase N has been crystallized by the vapour-diffusion method. Diffraction data have been collected and processed to 2.0 Å resolution. 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{sub 1}21, 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{sub M} value of 3.62 Å{sup 3} Da{sup −1}. Diffraction data were collected to 2.0 Å resolution using Cu Kα radiation from a rotating-anode X-ray generator.

• OSTI ID: 22360193
• Journal Information: Acta Crystallographica. Section F, Vol. 62, Issue Pt 7; Other Information: PMCID: PMC2242940; PMID: 16820698; PUBLISHER-ID: bw5149; OAI: oai:pubmedcentral.nih.gov:2242940; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AMMONIUM SULFATES
ANODES
CRYSTALLIZATION
CRYSTALS
DIFFRACTION
DIFFUSION
ESCHERICHIA COLI
MOLECULAR WEIGHT
MOLECULES
RESOLUTION
SPACE GROUPS