title: Purification and crystallization of Lactobacillus casei folylpolyglutamate synthetase expressed in Escherichia coli.
abstract: Folylpolyglutamate synthetase (FPGS) from Lactobacillus casei has been crystallized with polyethylene glycol and acetate buffer at pH 5.0. The enzyme was obtained from Escherichia coli strain SF4 harboring the L. casei FPGS chromosomal gene on a pEMBL vector (pGT3-8.1). Crystals of the enzyme were obtained which diffract to 2.6 A resolution. The crystals are monoclinic, space group P2(1), with unit cell dimensions of a = 54.07 A, b = 45.83 A, c = 84.37 A and beta = 107.92 degrees. A unit cell contains one molecule of the 43,000 Da enzyme per asymmetric unit. A complete X-ray data set on the native crystals has been collected.
authors.affiliation: Molecular Biophysics Department, Medical Foundation of Buffalo, NY 14203.
authors.forename: V
authors.initials: V
authors.lastname: Cody
authors.forename: J R
authors.initials: JR
authors.lastname: Luft
authors.forename: W
authors.initials: W
authors.lastname: Pangborn
authors.forename: J
authors.initials: J
authors.lastname: Toy
authors.forename: A L
authors.initials: AL
authors.lastname: Bognar
mesh_terms: D004926:Escherichia coli; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D010453:Peptide Synthases / Q000302:isolation & purification / Q000648:ultrastructure*; D011994:Recombinant Proteins; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D010453:Peptide Synthases; C023103:folylpolyglutamate synthetase