Ontology highlight
ABSTRACT:
SUBMITTER: Trillo-Muyo S
PROVIDER: S-EPMC4048058 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Trillo-Muyo Sergio S Jasilionis Andrius A Domagalski Marcin J MJ Chruszcz Maksymilian M Minor Wladek W Kuisiene Nomeda N Arolas Joan L JL Solà Maria M Gomis-Rüth F Xavier FX
Acta crystallographica. Section D, Biological crystallography 20130216 Pt 3
While small organic molecules generally crystallize forming tightly packed lattices with little solvent content, proteins form air-sensitive high-solvent-content crystals. Here, the crystallization and full structure analysis of a novel recombinant 10 kDa protein corresponding to the C-terminal domain of a putative U32 peptidase are reported. The orthorhombic crystal contained only 24.5% solvent and is therefore among the most tightly packed protein lattices ever reported. ...[more]