Small-angle scattering and the protein crystallographer: A relationship of ever-increasing interest
Author(s) -
David J. Scott
Publication year - 2014
Publication title -
the biochemist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.126
H-Index - 7
eISSN - 1740-1194
pISSN - 0954-982X
DOI - 10.1042/bio03601044
Subject(s) - domain (mathematical analysis) , construct (python library) , space (punctuation) , scattering , glycoprotein , high resolution , crystallography , small angle scattering , protein structure , resolution (logic) , chemistry , nanotechnology , computational biology , computer science , materials science , physics , biology , biochemistry , optics , geology , artificial intelligence , mathematics , mathematical analysis , remote sensing , programming language , operating system
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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