TY - JOUR T1 - Crystallization of the bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase domain of the human trifunctional enzyme. AU - Allaire,M, AU - Li,Y, AU - Mejia,N R, AU - Pelletier,J N, AU - MacKenzie,R E, AU - Cygler,M, PY - 1996/12/1/pubmed PY - 2000/6/20/medline PY - 1996/12/1/entrez SP - 479 EP - 80 JF - Proteins JO - Proteins VL - 26 IS - 4 N2 - Methylenetetrahydrofolate([H4] folate) dehydrogenase (D) and methenyl[H4] folate cyclohydrolase (C) coexist as a bifunctional enzyme (DC) or as the amino-terminal domain of a trifunctional enzyme (DCS) where the third activity is 10-formyl[H4]folate synthetase (S). Two crystal forms of the DC domain of the human cytosolic DCS enzyme have been grown from polyethyleneglycol solution. The monoclinic P2(1) crystals diffract to 2.8 A with a = 72.5 A, b = 68.5 A, c = 125.2 A, and beta = 91.8 degrees but were found to be twinned. The orthorhombic P2(1)2(1)2(1) crystals diffract to 2.5 A with a = 67.7 A, b = 135.9 A, c = 61.6 A, and contain two molecules per asymmetric unit. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/8990501/Crystallization_of_the_bifunctional_methylenetetrahydrofolate_dehydrogenase/methenyltetrahydrofolate_cyclohydrolase_domain_of_the_human_trifunctional_enzyme_ L2 - https://doi.org/10.1002/(SICI)1097-0134(199612)26:4<479::AID-PROT9>3.0.CO;2-6 DB - PRIME DP - Unbound Medicine ER -