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Crystallization of 3-hexulose-6-phosphate synthase Delfi, Masoud Mahdavian, Leila Sattarifar, Mohammad Hakulinen, Nina Rouvinen, Juha Protein crystallization Formaldehyde fixation Methylotrophic bacteria Methylomonas aminofaciens 77a 3-Hexulose-6-phosphate synthase Ribulose monophosphate pathway The crystal structures can reveal detailed information about the overall structure, active site structure, and functional mechanism of enzymes. This study focused on the crystallization of 3-hexulose-6-phosphate synthase from Methylomonas aminofaciens 77a, to produce higher resolution crystals for precise structural characterization. 3-Hexulose-6-phosphate synthase is from Methylomonas aminofaciens 77a (EC 4.1.2.43). It belongs to the orotidine 5'-monophosphate decarboxylase superfamily, and acts as a key enzyme for a ribulose-monophosphate cycle of formaldehyde fixation and detoxification. 3-Hexulose-6-phosphate synthase catalyzes the aldol condensation of formaldehyde with D-ribulose-5-phosphate. For the maximum activity, 3-hexulose-6-phosphate synthase requires Mg2+ or Mn2+ as ligands. MaHPS crystallized at the concentration of 7 mg/mL and conditions consisting of 0.2 M MgCl2, 18% PEG 3350 at pH = 7.0. Atlanta Publishing House LLC 2021-09-30 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion application/pdf https://www.eurjchem.com/index.php/eurjchem/article/view/2072 10.5155/eurjchem.12.3.299-303.2072 European Journal of Chemistry; Vol. 12 No. 3 (2021): September 2021; 299-303 2153-2257 2153-2249 eng https://www.eurjchem.com/index.php/eurjchem/article/view/2072/pdf_2072 Copyright (c) 2021 Authors