Preliminary X-ray Diffraction Analysis of Purine Nucleoside Phosphorylase from the Haloalkaliphilic Bacterium Halomonas chromatireducens-Reference-Cited by-同舟云学术

Preliminary X-ray Diffraction Analysis of Purine Nucleoside Phosphorylase from the Haloalkaliphilic Bacterium Halomonas chromatireducens

Published:2023-11-01 Issue:6 Volume:68 Page:922-925
ISSN:0023-4761
Container-title:Кристаллография
language:
Short-container-title:Kristallografiâ

Author:

Safonova T. N.¹,Antipov A. N.¹,Veiko V. P.¹,Mordkovich N. N.¹²,Okorokova N A.¹,Dorovatovskii P. V.³,Polyakov K. M.⁴

Affiliation:

1. Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia

2. Bochkov Research Centre for Medical Genetics, 115522, Moscow, Russia

3. National Research Centre “Kurchatov Institute”, 123098, Moscow, Russia

4. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia

Abstract

Crystals of the enzyme purine nucleoside phosphorylase from the extremophilic bacterium Halomonas Chromatireducens AGD 8-3, suitable for X-ray diffraction, were grown by the vapor-diffusion method. The X-ray diffraction data were collected from these crystals at the Belok beamline of the Kurchatov synchrotron radiation source (National Research Centre “Kurchatov Institute”) at 100 K to 1.80 Å resolution. The X-ray diffraction data were processed in the space groups P1, P2, P21, and P622. The structure was solved by the molecular replacement method taking into account the twinning in the space groups P21 and P1 with one and two hexamers of the enzyme per asymmetric unit, respectively.

Publisher

The Russian Academy of Sciences

Reference20 articles.

1. Ealick S.E., Rule S.A., Carter D.C. et al. // J. Biol. Chem. 1990. V. 265. P. 1812. https://doi.org/10.1016/S0021-9258(19)40090-2

2. Mao C., Cook W.J., Zhou M. et al. // Structure. 1997. V. 5. P. 1373. https://doi.org/10.1016/S0969-2126(97)00287-6

3. Krenitsky T.A., Koszalka G.W., Tuttle J.V. // Biochemistry. 1981. V. 20 (12). P. 3615. https://doi.org/10.1021/bi00515a048

4. Bennett E.M., Li C., Allan P.W. et al. // J. Biol. Chem. 2003. V. 278. P. 47110. https://doi.org/10.1074/jbc.M304622200

5. Ducati R.G., Santos D.S., Basso L.A. // Arch. Biochem. Biophys. 2009. V. 486. P. 155. https://doi.org/10.1016/j.abb.2009.04.011