Abstract
The methodology of protein crystallography provides a number of potential bottlenecks. Here, an approach to successful structure solution of a difficult heterodimeric complex of two human proteins, paraspeckle component 1 (PSPC1) and non-POU domain-containing octamer-binding protein (NONO), that are involved in gene regulation and the structural integrity of nuclear bodies termed paraspeckles is described. With the aid of bioinformatic predictions and systematic screening of a panel of constructs, bottlenecks of protein solubility, crystallization, crystal quality and crystallographic pseudosymmetry were overcome in order to produce crystals that ultimately revealed the structure.
Original language | English |
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Pages (from-to) | 981-987 |
Journal | Acta Crystallographica. Section D: Biological Crystallography |
Volume | 67 |
Issue number | 11 |
DOIs | |
Publication status | Published - 9 Nov 2011 |