Korean Journal of Crystallography (한국결정학회지)

Korean Crystallographic Association (한국결정학회)
권호 표지

Crystallization of 28 kDa Clonochis sinesis Glutathione S-transferase

  • Kim, Young-Kwan (School of Biological Sciences, Chungbuk National University) ;
  • Chung, Yong-Je (School of Biological Sciences, Chungbuk National University)
  • Published : 2003.06.01
Download PDF
⟨ Previous Next ⟩

Abstract

A helminth glutathione S-transferase. 28 kDa isozyme from Clonorchis sinensis has been crystallized under several conditions. One of the crystals, grown from a 10% polyehtylene glycol MME 550 (PEG MME 5 K) solution in 0.05 M potassium phosphate buffer (pH 7.0), diffracts to $3.0{\AA}$ resolution, and belongs to monoclinic space group C2, with unit cell parameters $a=95.83{\AA}$, $b=63.82{\AA}$, $c=235.09{\AA}$, and ${\beta}=97.2^{\circ}$.

여러 조건하에서 Clonorchis sinensis로부터 helminth glutatione S-transferase(28kDa isozyme)가 결정화되었다. 0.05 M potassium 완충 용액 (pH 7.0) 내에서 10% polyehtylene glycol MME 550(PEG MME 5 K)에서 자라난 결정이 $3.0{\AA}$ 분해능까지 회절하였다. 이 결정의 결정학적 자료는 다음과 같다 : 단사정계 공간 군 C2, $a=95.83{\AA}$, $b=63.82{\AA}$, $c=235.09{\AA}$, ${\beta}=97.2^{\circ}$.

Keywords

References

  1. Mannervik, B. and Danielson, U. H., CRC Crit. Rev. Biochem., 23, 283-337 (1988)
  2. Sheehan, D., Neade, G., Foley, V. M. and Dowd, C. A., Biochem. J., 360, 1-16 (2001)
  3. Pemble, S. E., Wardle, A. F. and Taylor, J. B., Biochem. J., 319, 749-754 (1996) https://doi.org/10.1042/bj3190749
  4. Board, P. G., Barker, R. T., Chelvanyagam, G. and Jermiin, L. S., Biochem. J., 328, 929-935 (1997)
  5. Brophy, P. M. and Barrett, J. Parasitology, 100, 345-349 (1990)
  6. O'eary, K. A., and Tracy, J. W., Exp. Parasitol., 72, 355-361 (1991)
  7. Kang, S. Y., Ahn, I-.Y., Park, C. Y., Chung, Y. B., Hong, S-.T., Kong, Y., Cho, S-.Y. and Hong, S-.J., Exp. Parasitol., 97, 186-195 (2001)
  8. Johnson, K. A., Angelucci, F., Bellelli, A., Herve, M., Fontaine, J., Tsernoglou, D., Capron, A., Trottein, F. and Brunori, M., Biochemistry, 42, 10084-10094 (2003)
  9. Simons, P. C. and van der Jagt, D. L., Anal. Biochem., 82, 334-337 (1977)
  10. Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J., J. Biol. Chem., 193, 265-275 (1951)
  11. Jancarik, J. and Kim, S. H. J. Appl. Crystallogr., 24, 409-411 (1991)
  12. Otwinowski, Z. and Minor, W., Methods Enzymol., 276, 307-325 (1997)
  13. Matthews, B. W., J. Mol. Biol., 33, 491-497 (1968)