Construct optimization for studying protein complexes: obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer

Mihwa Lee, Daniel Passon, Sven Hennig, Archa Fox, Charlie Bond

Research output: Contribution to journalArticle

14 Citations (Scopus)
285 Downloads (Pure)

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 languageEnglish
Pages (from-to)981-987
JournalActa Crystallographica. Section D: Biological Crystallography
Volume67
Issue number11
DOIs
Publication statusPublished - 9 Nov 2011

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