Crystallization and preliminary X‐ray characterization of prolyl tripeptidyl aminopeptidase from  Porphyromonas gingivalis | Zendy

Nakajima Yoshitaka | Zendy; Ito Kiyoshi | Zendy; Xu Yue | Zendy; Yamada Nozomi | Zendy; Onohara Yuko | Zendy; Ito Takashi | Zendy; Yoshimoto Tadashi | Zendy

Open Access

Crystallization and preliminary X‐ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis

Author(s) -

Nakajima Yoshitaka,

Ito Kiyoshi,

Xu Yue,

Yamada Nozomi,

Onohara Yuko,

Ito Takashi,

Yoshimoto Tadashi

Publication year - 2005

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309105035712

Subject(s) - porphyromonas gingivalis , crystallization , aminopeptidase , characterization (materials science) , chemistry , materials science , biochemistry , organic chemistry , bacteria , nanotechnology , biology , leucine , amino acid , genetics

A recombinant form of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis has been crystallized by the hanging‐drop vapour‐diffusion method using potassium sodium tartrate as a precipitating agent. The crystals belong to the hexagonal space group P 6 3 22, with unit‐cell parameters a = b = 149.4, c = 159.7 Å. The crystals are most likely to contain one subunit of a dimer in the asymmetric unit, with a V M value of 3.14 Å 3 Da −1 . Diffraction data were collected to 2.1 Å resolution using synchrotron radiation at the BL5 station of the Photon Factory.

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