| Literature DB >> 23519421 |
Sergio Trillo-Muyo1, Andrius Jasilionis, Marcin J Domagalski, Maksymilian Chruszcz, Wladek Minor, Nomeda Kuisiene, Joan L Arolas, Maria Solà, F Xavier Gomis-Rüth.
Abstract
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.Entities:
Keywords: crystal packing; high resolution; solvent content
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Year: 2013 PMID: 23519421 PMCID: PMC4048058 DOI: 10.1107/S0907444912050135
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449