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

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'...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-08, Vol.68 (8), p.883-888
Main Authors: Dolot, Rafal, Ozga, Magdalena, Wlodarczyk, Artur, Krakowiak, Agnieszka, Nawrot, Barbara
Format: Article
Language:English
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Summary: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 1.38Aa 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.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309112029491