Structural highlights
Function
G8N3E1_GEOTH
Publication Abstract from PubMed
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.
Ultratight crystal packing of a 10 kDa protein.,Trillo-Muyo S, Jasilionis A, Domagalski MJ, Chruszcz M, Minor W, Kuisiene N, Arolas JL, Sola M, Gomis-Ruth FX Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):464-70. doi:, 10.1107/S0907444912050135. Epub 2013 Feb 16. PMID:23519421[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Trillo-Muyo S, Jasilionis A, Domagalski MJ, Chruszcz M, Minor W, Kuisiene N, Arolas JL, Sola M, Gomis-Ruth FX. Ultratight crystal packing of a 10 kDa protein. Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):464-70. doi:, 10.1107/S0907444912050135. Epub 2013 Feb 16. PMID:23519421 doi:10.1107/S0907444912050135