Macromolecular powder diffraction: Ready for genuine biological problems

Knowledge of 3d structures of biological molecules plays a major role in both understanding important processes of life and developing pharmaceuticals. among several methods available for structure determination,macromolecular x-ray powder diffraction (xrpd) has transformed over the past decade from an impossible dream to a respectable method. xrpd can be employed in biosciences for various purposes such as observing phase transitions,characterizing bulk pharmaceuticals,determining structures via the molecular replacement method,detecting ligands in protein-ligand complexes,as well as combining micro-sized single crystal crystallographic data and powder diffraction data. studies using synchrotron and laboratory sources in some standard configuration setups are reported in this review,including their respective advantages and disadvantages. methods presented here provide an alternative,complementary set of tools to resolve structural problems. a variety of already existing software packages for powder diffraction data processing and analysis,some of which have been adapted to large unit cell studies,are briefly described. this review aims to provide necessary elements of theory and current methods,along with practical explanations,available software packages and highlighted case studies. © 2016 bentham science publishers.