Rafał Dolot, Magdalena Ozga, Artur Włodarczyk, Agnieszka Krakowiak, Barbara Nawrot
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引用次数: 0
Abstract
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 HINT1-adenosine 5'-monophosphate (AMP) complex at 1.38 Å resolution obtained from a new monoclinic crystal form is reported. The final structure has R(cryst) = 0.1207 (R(free) = 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.
期刊介绍:
Acta Crystallographica Section F is a rapid structural biology communications journal.
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