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Ultratight crystal packing of a 10 kDa protein.

Acta crystallographica. Section D, Biological crystallography (2013-03-23)
Sergio Trillo-Muyo, Andrius Jasilionis, Marcin J Domagalski, Maksymilian Chruszcz, Wladek Minor, Nomeda Kuisiene, Joan L Arolas, Maria Solà, F Xavier Gomis-Rüth
RÉSUMÉ

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.

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Seleno-DL-methionine, ≥99% (TLC)