title: A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 Å resolution.
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.
authors.affiliation: Department of Bioorganic Chemistry, Centre of Molecular and Macromolecular Studies, Sienkiewicza 112, 90-363 Łódź, Poland. rdolot@cbmm.lodz.pl
authors.forename: Rafał
authors.initials: R
authors.lastname: Dolot
authors.forename: Magdalena
authors.initials: M
authors.lastname: Ozga
authors.forename: Artur
authors.initials: A
authors.lastname: Włodarczyk
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Krakowiak
authors.forename: Barbara
authors.initials: B
authors.lastname: Nawrot
mesh_terms: D000249:Adenosine Monophosphate / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary
chemical_list: C063306:HINT1 protein, human; D009419:Nerve Tissue Proteins; D000249:Adenosine Monophosphate