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Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 01; 61(Pt 12):1046-8.AC

Abstract

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 P6(3)22, with unit-cell parameters a = b = 149.4, c = 159.7 A. The crystals are most likely to contain one subunit of a dimer in the asymmetric unit, with a VM value of 3.14 A3 Da(-1). Diffraction data were collected to 2.1 A resolution using synchrotron radiation at the BL5 station of the Photon Factory.

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Authors+Show Affiliations

Nakajima Y
Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Ito K
No affiliation info available
Xu Y
No affiliation info available
Yamada N
No affiliation info available
Onohara Y
No affiliation info available
Ito T
No affiliation info available
Yoshimoto T
No affiliation info available

MeSH

Bacterial ProteinsCrystallizationCrystallography, X-RayDimerizationDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEscherichia coliOpen Reading FramesPorphyromonas gingivalisProtein ConformationProtein Structure, TertiarySerine EndopeptidasesSynchrotrons

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16511231

Citation

Nakajima, Yoshitaka, et al. "Crystallization and Preliminary X-ray Characterization of Prolyl Tripeptidyl Aminopeptidase From Porphyromonas Gingivalis." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 61, no. Pt 12, 2005, pp. 1046-8.
Nakajima Y, Ito K, Xu Y, et al. Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005;61(Pt 12):1046-8.
Nakajima, Y., Ito, K., Xu, Y., Yamada, N., Onohara, Y., Ito, T., & Yoshimoto, T. (2005). Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 61(Pt 12), 1046-8.
Nakajima Y, et al. Crystallization and Preliminary X-ray Characterization of Prolyl Tripeptidyl Aminopeptidase From Porphyromonas Gingivalis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 1;61(Pt 12):1046-8. PubMed PMID: 16511231.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis. AU - Nakajima,Yoshitaka, AU - Ito,Kiyoshi, AU - Xu,Yue, AU - Yamada,Nozomi, AU - Onohara,Yuko, AU - Ito,Takashi, AU - Yoshimoto,Tadashi, Y1 - 2005/11/05/ PY - 2005/09/20/received PY - 2005/12/01/accepted PY - 2006/3/3/pubmed PY - 2006/6/3/medline PY - 2006/3/3/entrez SP - 1046 EP - 8 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 61 IS - Pt 12 N2 - 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 P6(3)22, with unit-cell parameters a = b = 149.4, c = 159.7 A. The crystals are most likely to contain one subunit of a dimer in the asymmetric unit, with a VM value of 3.14 A3 Da(-1). Diffraction data were collected to 2.1 A resolution using synchrotron radiation at the BL5 station of the Photon Factory. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/16511231/Crystallization_and_preliminary_X_ray_characterization_of_prolyl_tripeptidyl_aminopeptidase_from_Porphyromonas_gingivalis_ DB - PRIME DP - Unbound Medicine ER -