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170 MACROMOLECULAR CRYS TALLOGRAPHY

Its average value, recently jumped over 400,000 Å 3 Brunger, A. T., Adams, P. D., Clore, G. M., DeLano,
(1500 amino acid residues for the 50% solvent con- W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S.,
tent) may be affected by fewer giant structures Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J.,
such as the one for avian birnavirus (Coulibaly Rice, L. M., Simonson, T. and Warren, G. L. (1998).
et al., 2005) with 38 MDa content in the asymmetric Crystallography and NMR System: A new software
suite for macromolecular structure determination. Acta
unit. Although the unrefined model of this structure
Crystallogr. D 54, 905–921.
consists of approximately positioned Cα atoms into
Brunzelle, J. S., Shafaee, P., Yang, X., Weigand, S., Ren, Z.
a 7 Å density map, it does serve as an excellent
and Anderson, W. F. (2003). Automated crystallographic
example of the potential of macromolecular crystal- system for high-throughput protein structure determi-
lography for challenging projects. It is important, nation. Acta Crystallogr. D59, 1138–1144.
that the data for these and even more complicated Cohen, S. X., Morris, R. J., Fernandez, F. J., Jel-
structures are obtained using state-of-the-art tech- loul, M. B., Kakaris, M., Parthasarathy, V., Lamzin,
nologies and that the derived models present an as V. S., Kleywegt, G. J. and Perrakis, A. (2004).
accurate and complete interpretation as possible. Towards complete validated models in the next
generation of ARP/wARP. Acta Crystallogr. D 60,
2222–2229.
Coulibaly, F., Chevalier, C., Gutsche, I., Pous, J., Navaza, J.,
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