A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 A resolution

作者：Dolot Rafal^*; Ozga Magdalena; Wlodarczyk Artur; Krakowiak Agnieszka; Nawrot Barbara

来源：Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 2012, 68: 883-888.

DOI：10.1107/S1744309112029491

• HINT
• histidine triad nucleotide-binding proteins

Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch of the histidine triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the structure of the human HINT1adenosine 5'-monophosphate (AMP) complex at 1.38 angstrom resolution obtained from a new monoclinic crystal form is reported. The final structure has Rcryst = 0.1207 (Rfree = 0.1615) and the model exhibits good stereochemical quality. Detailed analysis of the high-resolution data allowed the details of the protein structure to be updated in comparison to the previously published data.

• 出版日期2012-8