Collect. Czech. Chem. Commun.
2005, 70, 124-132
https://doi.org/10.1135/cccc20050124
Crystallization and Preliminary X-ray Diffraction Analysis of Cold-Active β-Galactosidase from Arthrobacter sp. C2-2
Hana Petrokováa, Eva Vondráčkováa, Tereza Skálováa, Jan Dohnáleka, Petra Lipovováb, Vojtěch Spiwokb, Hynek Strnadb, Blanka Králováb and Jindřich Hašeka,*
a Institute of Macromolecular Chemistry, Academy of Sciences of the Czech Republic, Heyrovského nám. 2, 162 06 Prague 6, Czech Republic
b Department of Biochemistry, Institute of Chemical Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic
References
1. N. J.: Extremophiles 2000, 4, 83.
<https://doi.org/10.1007/s007920050141>
2. B.: Biochem. J. 1996, 316, 695.
<https://doi.org/10.1042/bj3160695>
3. R. H., Zhang X. J., DuBose R. F., Matthews B. W.: Nature 1994, 369, 761.
<https://doi.org/10.1038/369761a0>
4. D. H., Heightman T. D., Vasella A., McCarter J. D., Mackenzie L., Withers S. G., Matthews B. W.: Biochemistry 2001, 40, 14781.
<https://doi.org/10.1021/bi011727i>
5. M., Fushinobu S., Ohtsu N., Motoshima H., Matsuzawa H., Shoun H., Wakagi T.: J. Mol. Biol. 2002, 322, 79.
<https://doi.org/10.1016/S0022-2836(02)00746-5>
6. C. F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., Pearl L. H.: J. Mol. Biol. 1997, 271, 789.
<https://doi.org/10.1006/jmbi.1997.1215>
7. P. L., Wynn-Williams D. D., Russell N. J.: Antarct. Sci. 2000, 12, 386.
<https://doi.org/10.1017/S0954102000000432>
8. J., Gutshall K., Kasmir J., Prema P., Brenchley J. E.: Appl. Environ. Microbiol. 1994, 60, 12.
9. P., Spiwok V., Malá Š., Králová B., Russell N. J.: Czech J. Food Sci. 2002, 20, 43.
<https://doi.org/10.17221/3508-CJFS>
10. P., Strnad H., Spiwok V., Malá S., Králová B., Russell N. J.: Enzyme Microb. Technol. 2003, 33, 836.
<https://doi.org/10.1016/S0141-0229(03)00211-4>
11. F. M., Blakely B. T., Blau H. M.: Trends Cell Biol. 2000, 10, 119.
<https://doi.org/10.1016/S0962-8924(99)01707-9>
12. N., Feliu J. X., Vandevuer S., Muller A., Cabrera-Crespo J., Ortmans I., Hoffmann F., Cazorla D., Rinas U., Prevost M., Villaverde A.: J. Biol. Chem. 2001, 276, 40087.
<https://doi.org/10.1074/jbc.M104704200>
13. Z., Minor W.: Methods Enzymol. 1997, 276, 307.
<https://doi.org/10.1016/S0076-6879(97)76066-X>
14. A., Teplyakov A.: J. Appl. Crystallogr. 1997, 30, 1022.
<https://doi.org/10.1107/S0021889897006766>
15. B. W.: J. Mol. Biol. 1968, 28, 491.
<https://doi.org/10.1016/0022-2836(68)90205-2>
16. J.: Acta Crystallogr., Sect. A: Fundam. Crystallogr. 1994, 50, 157.
<https://doi.org/10.1107/S0108767393007597>
17. , No. 4: Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50, 760.
<https://doi.org/10.1107/S0907444994003112>
18. D. H., Jacobson R. H., Wigley D., Zhang X. J., Huber R. E., Tronrud D. E., Matthews B. W.: Protein Sci. 2000, 9, 1685.
<https://doi.org/10.1110/ps.9.9.1685>
19. D. E.: J. Struct. Biol. 1999, 125, 156.
<https://doi.org/10.1006/jsbi.1999.4094>
20. G. N., Vagin A. A., Dodson E. J.: Acta Crystallogr., Sect. D: Biol. Crystallogr. 1997, 53, 240.
<https://doi.org/10.1107/S0907444996012255>

