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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.

SUBMITTER: Trillo-Muyo S 

PROVIDER: S-EPMC4048058 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Ultratight crystal packing of a 10 kDa protein.

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]

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