Generation of High-Quality D-Dopachrome Tautomerase Crystals for Structural Studies.

Christopher Argueta, Georgios Pantouris

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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2 authors.

Christopher ArguetaDepartment of Chemistry, University of the Pacific, Stockton, CA, 95211, USA.

Georgios PantourisDepartment of Chemistry, University of the Pacific, Stockton, CA, 95211, USA. gpantouris@pacific.edu.

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6 · The paper itself

Abstract

Protein crystallography is a key technique of structural biology that allows researchers to determine the three-dimensional structure of proteins, protein-protein, protein-ligand, and protein-nucleic acid complexes at the atomic level. Whereas obtaining high-quality crystals is the first milestone for the structural characterization of a protein, the establishment of a detailed crystallization protocol promotes reproducibility of the crystallization process. Here, we describe a versatile crystallization method for human D-dopachrome tautomerase (D-DT or MIF-2), a small pleotropic protein of increasing interest due to its key role in human pathophysiology. The protocol described here provides a step-by-step procedure for generating high-quality protein crystals for a wide range of D-DT variants, including aggressive truncations and mutants with mechanistic value.

Indexed as

Intramolecular OxidoreductasesCrystallizationCrystallography, X-RayHumansProtein Conformationdopachrome isomeraseIntramolecular OxidoreductasesD-DTProtein crystallographyProtein crystalsProtein purificationX-ray crystallography

Identifiers

PMID42129110

DOI10.1016/j.xpro.2023.102375

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