title: Flexible nanoassembly for sequestering non-native proteins.
abstract: A crystal structure of a yeast small heat shock protein reported by Hanazono and colleagues in this issue of Structure reveals the versatility of the α-crystallin domain dimer for building assemblies of different size and symmetry. The domains assemble into a vessel filled with hydrophobic sequence extensions enriched with phenylalanines.
authors: Department of Biological Sciences, Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK. c.slingsby@mail.cryst.bbk.ac.uk
authors: Christine
authors: C
authors: Slingsby
authors: Alice R
authors: AR
authors: Clark
mesh_terms: D006360:Heat-Shock Proteins / Q000737:chemistry*; D012568:Schizosaccharomyces; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry*
chemical_list: D006360:Heat-Shock Proteins; D029702:Schizosaccharomyces pombe Proteins; C491888:hsp16 protein, S pombe