title: Molecular replacement.
abstract: As more protein structures are solved, the likelihood that current structural investigations will involve proteins for which there exists no homologous structure continually decreases. The extraction of phase information from diffraction experiments is one of several great barriers that crystallographers must overcome on the path to structure solution. One means to overcome this obstacle, the technique of molecular replacement, uses the structural similarity between proteins with similar sequences to give a good first estimate of the phases for the diffraction data of the protein of interest. The programs that execute this technique currently come in many flavors, from traditional Patterson-based methods, to stochastic searches in greater than three dimensions, to maximum likelihood-enhanced molecular replacement, each possessing unique advantages that can shake loose a recalcitrant solution. As crystallographers aim to solve larger macromolecular complexes that more faithfully depict the actors in cellular events, having existing phase information for parts of those biological machines will reinforce the technological advancements in data collection and structure solution that have already produced mammoth structures like the ribosome, yielding an ever-clearer picture of the inner workings of biology.
authors.affiliation: Department of Biochemistry and Molecular Biology, Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD, USA.
authors.forename: Eric A
authors.initials: EA
authors.lastname: Toth
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins