title: Ultratight crystal packing of a 10 kDa protein.
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.
authors.affiliation: Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Spanish Research Council CSIC, Barcelona Science Park, c/Baldiri Reixac 15-21, 08028 Barcelona, Spain.
authors.forename: Sergio
authors.initials: S
authors.lastname: Trillo-Muyo
authors.forename: Andrius
authors.initials: A
authors.lastname: Jasilionis
authors.forename: Marcin J
authors.initials: MJ
authors.lastname: Domagalski
authors.forename: Maksymilian
authors.initials: M
authors.lastname: Chruszcz
authors.forename: Wladek
authors.initials: W
authors.lastname: Minor
authors.forename: Nomeda
authors.initials: N
authors.lastname: Kuisiene
authors.forename: Joan L
authors.initials: JL
authors.lastname: Arolas
authors.forename: Maria
authors.initials: M
authors.lastname: Solà
authors.forename: F Xavier
authors.initials: FX
authors.lastname: Gomis-Rüth
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D056506:Geobacillus / Q000201:enzymology*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry*; D059748:Proteolysis; D012645:Selenomethionine / Q000378:metabolism; D012997:Solvents
chemical_list: D010446:Peptide Fragments; D012997:Solvents; D012645:Selenomethionine; D010447:Peptide Hydrolases
keywords: crystal packing; high resolution; solvent content