Three-dimensional structure of β-galactosidase from E. coli.

Nature

Volumn 369, Issue 6483, 1994, Pages 761-766

  Jacobson, R H ^a   Zhang, X J ^a   Dubose, R F ^b   Matthews, B W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; BETA-GALACTOSIDASE; COMPUTER GRAPHICS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; IMAGE PROCESSING, COMPUTER-ASSISTED; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, U.S. GOV'T, P.H.S.;

ESCHERICHIA COLI;

EID: 0028178377     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/369761a0     Document Type: Article

References (32)

1. Jacob, F. & Monod, J. J. molec. Biol. 3, 318-356 (1961).
2. Fowler, A. & Zabin, I. J. biol. Chem. 253, 5521-5525 (1978).
3. Kalnins, A., Otto, K., Ruther, U. & Müller-Hill, B. EMBO J. 2, 593-597 (1983).
4. Jacobson, R. H. & Matthews, B. W. J. molec. Biol. 223, 1177-1182 (1992).
5. Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. Acta crystallogr. A43, 489-501 (1987).
6. Holmgren, A. & Bränden, C. I. Nature. 342, 248-251 (1989).
7. Brändén, C. Q. Rev. Biophys. 13, 317-330 (1980).
8. Matthews, B. W., Jansonius, J. N., Colman, P. M., Schoenborn, B. P. & Dupourque, D. Nature New Biol. 238, 37-41 (1972).
9. Celacla, F., Ullmann, A. & Monod, J. Biochemistry. 13, 5543-5547 (1974).
10. Ring, M. & Huber, R. E. Arch. Biochem. Biophys. 283, 342-350 (1990).
11. Gebier, J. C., Aebersold, R. & Withers, S. G. J. biol. Chem. 267, 11126-11130 (1992).
12. Cupples, C. G., Miller, J. H. & Huber, R. E. J. biol. Chem. 265, 5512-5518 (1990).
13. Ullmann, A., Jacob, F. & Monod, J. J. molec. Biol. 24, 339-343 (1967).
14. Langley, K. E., Viilarejo, M. R., Fowler, A. V., Zamenhof, P. J. & Zabin, I. Proc. natn. Acad. Sci. U.S.A. 72, 1254-1257 (1975).
15. Weinstock, G. M., Berman, M. L. & Silhavy, T. J. in Gene Amplification and Analysis. (eds Papes, T. S., Rosenberg, M. & Chirikjian, J. G.) 27-64 (Elsevier, New York, 1983).
16. Zabin, I. Molec. cell. Biochem. 49, 87-96 (1982).
17. Henderson, D. R., Friedman, S. B., Harris, J. D., Manning, W. B. & Zoccoli, M. A. Clin. Chem. 32, 1637-1641 (1986).
18. Adams, R. M. et al. J. biol. Chem. 269, 5666-5672 (1994).
19. Heinz, D. W. & Matthews, B. W. Prot. Engng. 7, 301-307 (1994).
20. Sakabe, N. Nucl. Inst. Meth. A303, 448-463 (1991).
21. Higashi, T. J. appl. Cryst 22, 9-18 (1989).
22. TerwiNiger, T. & Eisenberg, D. Acta crystallogr. A39, 813-817 (1983).
23. Rayment, I. Acta crystallogr. A39, 102-116 (1983).
24. Kraulls, P. J. J. appl. Cryst. 24, 946-950 (1991).
25. Kabsch, W. & Sander, C. Biopolymers 22, 2577-2637 (1983).
26. Stokes, H. W., Betts, P. W. & Hall, B. G. Molec. Biol. Evol. 2, 469-477 (1985).
27. Buvinger, W. E. & Riiey, M. J. Bact. 163, 850-957 (1985).
28. Schroeder, C. J., Robert, C., Lenzen, G., McKay, L. L. & Mercenier, A. J. gen. Microbiol. 137, 369-380 (1991).
29. Schmidt, B. F., Adams, R. M., Requadt, C., Power, S. & Mainzer, S. E. J. Bact. 171, 625-635 (1989).
30. Hancock, K. R. et al. J. Bact. 173, 3084-3095 (1991).
31. Gaykema, W. P. J. et al. Nature. 309, 23-29 (1984).
32. Rossmann, M. G. et al. Nature. 317, 145-153 (1985).