Understanding the function of proteins requires characterizing their structure as well as their dynamics. Thousands of "rigid" structures exist in databases, but relatively little information is available on their dynamics. Recent advances in crystallography make it possible to obtain this information, regarding the movements of proteins in their crystals. Nevertheless, there is one central question that has barely been investigated: how does the packing of proteins in the crystal influence protein dynamics?
Researchers from the IBS, in collaboration with Purdue University (USA), have used a combination of novel approaches in solid-state NMR spectroscopy and lengthy molecular dynamics simulations to clarify this question. This study revealed that the movements of a protein at biologically important time scales are indeed influenced by crystalline packing. These results are important for future research into molecular dynamics by crystallography.