Considerations for the refinement of low-resolution crystal structures

Acta Crystallographica Section D: Biological Crystallography

Volumn 62, Issue 8, 2006, Pages 923-932

  DeLaBarre, Byron ^a,b   Brunger, Axel T ^a,b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATASES; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY;

EID: 33746414364     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444906012650     Document Type: Article

References (29)

1. Adams, P. D., Pannu, N. S., Read, R. J. & Brünger, A. T. (1997). Proc. Natl Acad. Sci. USA, 94, 5018-5023.
2. Adams, P. D., Pannu, N. S., Read, R. J. & Brunger, A. T. (1999). Acta Cryst. D55, 181-190.
3. Afonine, P. V., Grosse-Kunstleve, R. W. & Adams, P. D. (2005). Acta Cryst. D61, 850-855.
4. Aishima, J., Russel, D. S., Guibas, L. J., Adams, P. D. & Brunger, A. T. (2005). Acta Cryst. D61, 1354-1363.
5. Ban, N., Nissen, P., Hansen, J., Moore, P. B. & Steitz, T. A. (2000). Science, 289, 905-920.
6. Bass, R. B., Strop, P., Barclay, M. & Rees, D. C. (2002). Science, 298, 1582-1587.
7. Chen, B., Vogan, E. M., Gong, H., Skehel, J. J., Wiley, D. C. & Harrison, S. C. (2005). Structure, 13, 197-211.
8. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
9. DeLaBarre, B. & Brunger, A. T. (2003). Nature Struct. Biol. 10, 856-863.
10. DeLaBarre, B. & Brunger, A. T. (2005). J. Mol. Biol. 347, 437-452.
11. Hausrath, A. C., Capaldi, R. A. & Matthews, B. W. (2001). J. Biol. Chem. 276, 47227-47232.
12. Heldwein, E. E., Macia, E., Wang, J., Yin, H. L., Kirchhausen, T. & Harrison, S. C. (2004). Proc. Natl Acad. Sci. USA, 101, 14108-14113.
13. Huyton, T., Pye, V. E., Briggs, L. C., Flynn, T. C., Beuron, F., Kondo, H., Ma, J., Zhang, X. & Freemont, P. S. (2003). J. Struct. Biol. 144, 337-348.
14. Jaeger, J., Restle, T. & Steitz, T. A. (1998). EMBO J. 17, 4535-4542.
15. Jiang, J. S. & Brünger, A. T. (1994). J. Mol. Biol. 243, 100-115.
16. Jin, R., Junutula, J. R., Matern, H. T., Ervin, K. E., Scheller, R. H. & Brunger, A. T. (2005). EMBO J. 24, 2064-2074.
17. Lacy, D. B., Wigelsworth, D. J., Melnyk, R. A., Harrison, S. C. & Collier, R. J. (2004). Proc. Natl Acad. Sci. USA, 101, 13147-13151.
18. Laskowski, R. (1993). J. Appl. Cryst. 26, 283-291.
19. Ling, H., Boodhoo, A., Hazes, B., Cummings, M. D., Armstrong, G. D., Brunton, J. L. & Read, R. J. (1998). Biochemistry, 37, 1777-1788.
20. Momany, C., Kovari, L. C., Prongay, A. J., Keller, W., Gitti, R. K., Lee, B. M., Gorbalenya, A. E., Tong, L., McClure, J., Ehrlich, L. S., Summers, M. F., Carter, C. & Rossmann, M. G. (1996). Nature Struct. Biol. 3, 763-770.
21. Pannu, N. S., Murshudov, G. N., Dodson, E. J. & Read, R. J. (1998). Acta Cryst. D54, 1285-1294.
22. Perrakis, A., Morris, R. & Lamzin, V. S. (1999). Nature Struct. Biol. 6, 458-463.
23. Rice, L. M., Earnest, T. N. & Brunger, A. T. (2000). Acta Cryst. D56, 1413-1420.
24. Rouiller, I., DeLaBarre, B., May, A. P., Weis, W. I., Brunger, A. T., Milligan, R. A. & Wilson-Kubalek, E. M. (2002). Nature Struct. Biol. 9, 950-957.
25. Terwilliger, T. (2003). Acta Cryst. D59, 1174-1182.
26. Vila-Sanjurjo, A., Ridgeway, W. K., Seymaner, V., Zhang, W., Santoso, S., Yu, K. & Cate, J. H. (2003). Proc. Natl Acad. Sci. USA, 100, 8682-8687.
27. Wang, J. H., Meijers, R., Xiong, Y., Liu, J. H., Sakihama, T., Zhang, R., Joachimiak, A. & Reinherz, E. L. (2001). Proc. Natl Acad. Sci. USA, 98, 10799-10804.
28. Yonath, A., Müssig, J., Tesche, B., Lorenz, S., Erdmann, V. A. & Wittmann, H. G. (1980). Biochem. Int. 2, 428-430.
29. Zhang, X., Shaw, A., Bates, P. A., Newman, R. H., Gowen, B., Orlova, E., Gorman, M. A., Kondo, H., Dokurno, P., Lally, J., Leonard, G., Meyer, H., van Heel, M. & Freemont, P. S. (2000). Mol. Cell, 6, 1473-1484.