Table 1.
Advantages and limiations of experimental structure determination techniques.
| Large proteins and complexes High resolution structures |
Requires high protein concentration Possible crystallographic artifacts: packing, non-native conformatins Ad hoc detemination of crystalizing conditions for the target protein Limited to stable proteins Molecular motion is challenging to obtain |
| Multiple complementary techniques for structure determination: two (and higher)-dimensional NMR, residual dipolar coupling, hydrogen-deuterium exchange, paramagnetic relaxation enhancements Ability to quantify dynamics and witness large-scale conformational dynamics of proteins |
Requires high protein concentration Atominc assignment may present challenges |
| Large structures Ability to witness many conformational states Fairly rapid workflow |
Small proteins still present a challenge |