Generalized X-ray and neutron crystallographic analysis: More accurate and complete structures for biological macromolecules

Acta Crystallographica Section D: Biological Crystallography

Volumn 65, Issue 6, 2009, Pages 567-573

  Adams, Paul D ^a,b   Mustyakimov, Marat ^c   Afonine, Pavel V ^a   Langan, Paul ^c  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b University of California at Berkeley   (United States)

^c LOS ALAMOS NATIONAL LABORATORY   (United States)

Author keywords

Joint X ray and neutron crystallography; Structure refinement

Indexed keywords

BACTERIAL PROTEIN; DIISOPROPYL FLUOROPHOSPHATASE; DIISOPROPYL-FLUOROPHOSPHATASE; PHOSPHOTRIESTERASE; PHOTOACTIVE YELLOW PROTEIN, BACTERIA; VISUAL PROTEINS AND PIGMENTS;

ARTICLE; BIOLOGY; CHEMISTRY; COMPARATIVE STUDY; ESCHERICHIA COLI; FEASIBILITY STUDY; MACROMOLECULE; METHODOLOGY; NEUTRON DIFFRACTION; PROTEIN CONFORMATION; REPRODUCIBILITY; TEMPERATURE; THEORETICAL MODEL; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; COMPUTATIONAL BIOLOGY; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FEASIBILITY STUDIES; MACROMOLECULAR SUBSTANCES; MODELS, THEORETICAL; NEUTRON DIFFRACTION; PHOSPHORIC TRIESTER HYDROLASES; PHOTORECEPTORS, MICROBIAL; PROTEIN CONFORMATION; REPRODUCIBILITY OF RESULTS; TEMPERATURE;

EID: 66249139220     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444909011548     Document Type: Article

References (21)

1. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, X C., Sauter, N. K. & Terwilliger, T. C. (2002). Acta Cryst. D58, 1948-1954.
2. Brünger, A. T. (1992). Nature (London), 355, 472-475.
3. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
4. Dasgupta, S., Iyer, G. H., Bryant, S. H., Lawrence, C. E. & Bell, X A. (1997). Proteins, 28, 494-514.
5. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
6. Freudenthal, B. D., Ramaswamy, S., Hingorani, M. M. & Washington, M. T. (2008). Biochemistry, 47, 13354-13361.
7. Hingorani, M. M. & O'Donnell, M. (2000). Curr. Biol. 10, R25-R29.
8. Indiani, C. & O'Donnell, M. (2006). Nature Rev. Mol. Cell Biol. 7, 751-761.
9. Krishna, T. S., Kong, X. P., Gary, S., Burgers, P. M. & Kuriyan, X (1994). Cell, 79, 1233-1243.
10. Maga, G. & Hübscher, U. (2003). J. Cell Sci. 116, 3051-3060.
11. Majka, X & Burgers, P. M. (2004). Prog. Nucleic Acid Res. Mol. Biol. 78, 227-260.
12. Matsumiya, S., Ishino, S., Ishino, Y. & Morikawa, K. (2003). Protein Sci. 12, 823-831.
13. Matsumiya, S., Ishino, Y. & Morikawa, K. (2001). Protein Sci. 10, 17-23.
14. Moldovan, G.-L., Pfander, B. & Jentsch, S. (2007). Cell, 129, 665-679.
15. Mossi, R. & Hübscher, U. (1998). Eur. J. Biochem. 254, 209-216.
16. Naryzhny, S. N. (2008). Cell. Mol. Life Sci. 65, 3789-3808.
17. Northam, M. R., Garg, P., Baitin, D. M., Burgers, P. M. X & Shcherbakova, P. V. (2006). EMBO J. 25, 4316-4325.
18. Pflugrath, X W. (1999). Acta Cryst. D55, 1718-1725.
19. Read, R. X (2001). Acta Cryst. D57, 1373-1382.
20. Tsurimoto, T. (1999). Front. Biosci. 4, d849-d858.
21. Zhang, P., Zhang, S.-J., Zhang, Z., Woessner, X F. & Lee, M. Y. W. T. (1995). Biochemistry, 34, 10703-10712.