title: Assessment of protein structure refinement in CASP9.
abstract: We assess performance in the structure refinement category in CASP9. Two years after CASP8, the performance of the best groups has not improved. There are few groups that improve any of our assessment scores with statistical significance. Some predictors, however, are able to consistently improve the physicality of the models. Although we cannot identify any clear bottleneck in improving refinement, several points arise: (1) The refinement portion of CASP has too few targets to make many statistically meaningful conclusions. (2) Predictors are usually very conservative, limiting the possibility of large improvements in models. (3) No group is actually able to correctly rank their five submissions-indicating that potentially better models may be discarded. (4) Different sampling strategies work better for different refinement problems; there is no single strategy that works on all targets. In general, conservative strategies do better, while the greatest improvements come from more adventurous sampling-at the cost of consistency. Comparison with experimental data reveals aspects not captured by comparison to a single structure. In particular, we show that improvement in backbone geometry does not always mean better agreement with experimental data. Finally, we demonstrate that even given the current challenges facing refinement, the refined models are useful for solving the crystallographic phase problem through molecular replacement. Proteins 2011;. © 2011 Wiley-Liss, Inc.
authors: Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, New York, USA. justin.maccallum@me.com.
authors: Justin L
authors: JL
authors: MacCallum
authors: Alberto
authors: A
authors: Pérez
authors: Michael J
authors: MJ
authors: Schnieders
authors: Lan
authors: L
authors: Hua
authors: Matthew P
authors: MP
authors: Jacobson
authors: Ken A
authors: KA
authors: Dill
mesh_terms: D019295:Computational Biology / Q000379:methods*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012984:Software
chemical_list: D011506:Proteins