Protein crystallography is one of the great intellectual achievements of the 20th Century, and it continues to open up new vistas of research as scientists are able to visualize in exquisite detail the molecules of Life. It has become increasingly apparent, however, that not all proteins are amenable to crystallographic analysis. These include (but are not confined to) proteins with functional flexible segments, glycoproteins and intrinsically disordered proteins. There are also proteins that, although rigid and folded, refuse to crystallize as an entire full-length construct, and hence high-resolution information has to be pieced together domain by domain. It is into this space that small-angle scattering is increasingly being used as the technique of choice with regard to attainable structural information.
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Feature| February 01 2014
Small-angle scattering and the protein crystallographer: A relationship of ever-increasing interest
Biochem (Lond) (2014) 36 (1): 44–48.
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David J. Scott; Small-angle scattering and the protein crystallographer: A relationship of ever-increasing interest. Biochem (Lond) 1 February 2014; 36 (1): 44–48. doi: https://doi.org/10.1042/BIO03601044
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