More efficient protein structure determination is a major goal of the US structural genomics projects. X-ray crystallography shines in its ability to determine structures quickly from data gathered at synchrotron beam lines, but only a fraction of proteins that can be produced in soluble form crystallize to yield X-ray structures. Many smaller proteins that fail in crystallization trials can yield solution structures by nuclear magnetic resonance (NMR), however.
NMR structures are fundamentally different from their X-ray-derived counterparts. For one thing, the proteins are in solution rather than locked in crystals; the resulting structures are thus more reflective of the molecules' natural (in vivo) state. Moreover, NMR provides something X-ray structures cannot: valuable information about protein dynamics, chemical properties, and ligand binding.
But NMR has problems, too. The process is computationally intensive, and bottlenecks in data collection and analysis mean structure determination can take weeks or even months. Now we and ...
