Crystal structure of the Aequorea victoria green fluorescent protein

Science

Volumn 273, Issue 5280, 1996, Pages 1392-1395

  Ormö, Mats ^a   Cubitt, Andrew B ^b   Kallio, Karen ^a   Gross, Larry A ^c   Tsien, Roger Y ^c   Remington, S James ^a  

^a UNIVERSITY OF OREGON   (United States)

^b Aurora Biosciences Corporation   (United States)

^c San Diego   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; GENE EXPRESSION; JELLYFISH; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0029847806     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5280.1392     Document Type: Article

References (43)

1. O. Shimomura and F. H. Johnson, J. Cell. Comp, Physiol. 59, 223 (1962); J, G. Morin and J. W. Hastings, J. Cell. Physiol. 77, 313 (1971); H. Morise, O. Shimomura, F. H. Johnson, J. Winant, J. Biochem. 13, 2656 (1974); W, W. Ward, Photochem. Photobiol. Rev. 4, 1 (1979).
2. O. Shimomura and F. H. Johnson, J. Cell. Comp, Physiol. 59, 223 (1962); J, G. Morin and J. W. Hastings, J. Cell. Physiol. 77, 313 (1971); H. Morise, O. Shimomura, F. H. Johnson, J. Winant, J. Biochem. 13, 2656 (1974); W, W. Ward, Photochem. Photobiol. Rev. 4, 1 (1979).
3. O. Shimomura and F. H. Johnson, J. Cell. Comp, Physiol. 59, 223 (1962); J, G. Morin and J. W. Hastings, J. Cell. Physiol. 77, 313 (1971); H. Morise, O. Shimomura, F. H. Johnson, J. Winant, J. Biochem. 13, 2656 (1974); W, W. Ward, Photochem. Photobiol. Rev. 4, 1 (1979).
4. O. Shimomura and F. H. Johnson, J. Cell. Comp, Physiol. 59, 223 (1962); J, G. Morin and J. W. Hastings, J. Cell. Physiol. 77, 313 (1971); H. Morise, O. Shimomura, F. H. Johnson, J. Winant, J. Biochem. 13, 2656 (1974); W, W. Ward, Photochem. Photobiol. Rev. 4, 1 (1979).
5. D. C. Prasher, V. K, Eckenrode, W. W, Ward, F, G. Prendergast, M. J, Cormier, Gene 111, 229 (1992).
6. M. Chalfie, Y. Tu, G. Euskirchen, W. W. Ward, D. C. Prasher, Science 263, 802 (1994).
7. A. B. Cubitt et al., Trends Biochem. Sci. 20, 448 (1995)
8. D. C. Prasher, Trends Genet. 11, 320 (1995); M. Chalfie, Photochem. Photobiol. 62, 651 (1995).
9. D. C. Prasher, Trends Genet. 11, 320 (1995); M. Chalfie, Photochem. Photobiol. 62, 651 (1995).
10. W. W. Ward, in Bioluminescence and Chemiluminescence, M. A. DeLuca and W. D. McElroy, Eds. (Academic Press, New York, 1981), pp. 235-242; -and S. H. Bokman, Biochemistry 21, 4535 (1982); W. W. Ward et al, Photochem. Photobiol. 35, 803 (1982).
11. W. W. Ward, in Bioluminescence and Chemiluminescence, M. A. DeLuca and W. D. McElroy, Eds. (Academic Press, New York, 1981), pp. 235-242; -and S. H. Bokman, Biochemistry 21, 4535 (1982); W. W. Ward et al, Photochem. Photobiol. 35, 803 (1982).
12. W. W. Ward, in Bioluminescence and Chemiluminescence, M. A. DeLuca and W. D. McElroy, Eds. (Academic Press, New York, 1981), pp. 235-242; -and S. H. Bokman, Biochemistry 21, 4535 (1982); W. W. Ward et al, Photochem. Photobiol. 35, 803 (1982).
13. C. W. Cody, D. C. Prasher, W. M. Westler, F. G. Prendergast, W. W. Ward, Biochemistry 32, 1212 (1993).
14. R, Heim, D. C. Prasher, R. Y. Tsien, Proc. Natl. Acad. Sci. U.S.A. 91, 12501 (1994).
15. Abbreviations for the amino acid residues are as follows; A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, lle; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
16. R. Heim, A. B. Cubitt, R. Y. Tsien, Nature 373, 664 (1995).
17. 1 with a = 51.8, b = 62.8, C = 70.7 Å, Z = 4. Two crystal forms of wild-type GFP, unrelated to the present form, have been described by M. A. Perrozo, K. B. Ward, R. B. Thompson, and W. W. Ward [J. Biol. Chem. 203, 7713 (1988)].
18. J. Dopf and T. M. Horiagon, Gene 173, 39 (1996).
19. B. D. Nageswara Rao, M. D. Kemple, F. G. Prendergast, Biophys. J. 32, 630 (1980).
20. B. Lee and F. M. Richards, J. Mol. Biol. 55, 379 (1971). The atomic radii were those of Lee and Richards, calculated by use of the program MS with a probe radius of 1.4 Å. [M. L. Connolly, Science 221, 709 (1983)].
21. B. Lee and F. M. Richards, J. Mol. Biol. 55, 379 (1971). The atomic radii were those of Lee and Richards, calculated by use of the program MS with a probe radius of 1.4 Å. [M. L. Connolly, Science 221, 709 (1983)].
22. S. J. Hubbard, K.-H. Gross, P. Argos, Protein Eng. 7, 613 (1994); A. E. Eriksson et al., Science 255, 178 (1992).
23. S. J. Hubbard, K.-H. Gross, P. Argos, Protein Eng. 7, 613 (1994); A. E. Eriksson et al., Science 255, 178 (1992).
24. S. Inouye and F, I. Tsuji, FEBS Lett. 351 , 211 (1994).
25. 48.
26. 2H and the finite resolution of the Hewlett-Packard 5989B electrospray mass spectrometer used to make these measurements do not permit the individual peaks to be resolved, but instead yield an average mass peak with a full width at half maximum of 55 daltons. The molecular sizes shown include the His-tag, which has the sequence MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDPPAEF (9, 10).
27. T. Ehrig, D. J. O'Kane, F. G. Prendergast, FEBS Lett. 367, 163 (1995).
28. S. Delagrave, R. E. Hawtin, C. M. Silva, M. M. Yang, D. C. Youvan, Bio/Technology 13, 151 (1995).
29. R. Heim and R. Y. Tsien, Curr. Biol. 6, 178 (1996).
30. R. M. San Pietro, F. G. Prendergast, W. W. Ward, Photochem. Photobiol. 57, s63 (1993).
31. G. E. O. Borgstahl, D. R. Williams, E. D. Getzoff, Biochemistry 34, 6278 (1995).
32. F. Yang, L. G. Moss, G. N. Phillips, Nature Biotechnol., in press.
33. Z. Otwinowski, in Proceedings of the CCP4 Study Weekend: Data Collection and Processing, L. Sawyer, N. Issacs, S. Bailey, Eds. (Science and Engineering Research Council, Daresbury Laboratory, Warrington, UK, 1991), pp. 56-62; W. Minor, XDISPLAYF (Purdue University, West Lafayette, IN, 1993).
34. Z. Otwinowski, in Proceedings of the CCP4 Study Weekend: Data Collection and Processing, L. Sawyer, N. Issacs, S. Bailey, Eds. (Science and Engineering Research Council, Daresbury Laboratory, Warrington, UK, 1991), pp. 56-62; W. Minor, XDISPLAYF (Purdue University, West Lafayette, IN, 1993).
35. A. J. Howard, C. Nielsen, N. H. Xuong, Methods Enzymol. 114, 452 (1985).
36. W. Steigemann, thesis, Technical University, Munich (1974).
37. CCP4: A Suite of Programs for Protein Crystallography (Science and Engineering Research Council, Daresbury Laboratory, Warrington, UK, 1979).
38. T. A. Jones, J.-Y. Zou, S. W. Cowan, M. Kjelgaard, Acta Crystallogr. Sect. A 47, 110 (1991); T. A. Jones, in Computational Crystallography, D. Sayre, Ed. (Oxford Univ. Press, Oxford, 1982), pp. 303-317.
39. T. A. Jones, J.-Y. Zou, S. W. Cowan, M. Kjelgaard, Acta Crystallogr. Sect. A 47, 110 (1991); T. A. Jones, in Computational Crystallography, D. Sayre, Ed. (Oxford Univ. Press, Oxford, 1982), pp. 303-317.
40. D. E. Tronrud, L. F, Ten Eyck, B. W. Matthews, Acta Crystallogr. Sect. A 43, 489 (1987).
41. B. P. Cormack, R. H. Valdivia, S. Falkow, Gene 173, 33 (1996)
42. P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991).
43. We thank T. Ross for initial crystallization of GFP; M. Sagermann for help with the CCP4 package for crystallographic computing; and M. Elsliger, C. Ogata, and R. Brennan for help with data collection. Facilities at the University of Oregon and beamline X4A at the Brookhaven National Laboratory are supported in part by the Howard Hughes Medical Institute and a grant from the National Science Foundation (MCB 9418479) to S.J.R. M.O. gratefully acknowledges the Swedish Natural Science Research Council for a postdoctoral fellowship.