A new crystal form of human histidine triad nucleotide‐binding protein 1 (hHINT1) in complex with adenosine 5′‐monophosphate at 1.38 Å resolution | Zendy

Dolot Rafał | Zendy; Ozga Magdalena | Zendy; Włodarczyk Artur | Zendy; Krakowiak Agnieszka | Zendy; Nawrot Barbara | Zendy

Open Access

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

Author(s) -

Dolot Rafał,

Ozga Magdalena,

Włodarczyk Artur,

Krakowiak Agnieszka,

Nawrot Barbara

Publication year - 2012

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309112029491

Subject(s) - histidine , triad (sociology) , resolution (logic) , nucleotide , chemistry , monoclinic crystal system , adenosine monophosphate , crystallography , high resolution , helix (gastropod) , stereochemistry , adenosine , biochemistry , crystal structure , biology , enzyme , computer science , psychology , artificial intelligence , psychoanalysis , gene , ecology , remote sensing , snail , geology

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.

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