title: Crystallization and preliminary cryogenic X-ray diffraction analyses of protein L-isoaspartyl O-methyltransferase from human fetal brain.
abstract: Recombinant human fetal brain protein L-isoaspartyl O-methyltransferase, EC 2.1.1.77, was crystallized in PEG 8000 with adenosine homocysteine by a macroseeding technique. The space group was P2(1) with a = 47.4 A, b = 53.9 A, c = 48.7 A and beta = 116.4 degrees for cryofrozen crystals at 90 K. The crystals diffracted to 2.1 A and have one molecule per asymmetric unit.
authors.affiliation: Center for Macromolecular Crystallography, University of Alabama at Birmingham, USA.
authors.forename: C D
authors.initials: CD
authors.lastname: Smith
authors.forename: J
authors.initials: J
authors.lastname: Barchue
authors.forename: C
authors.initials: C
authors.lastname: Mentel
authors.forename: L
authors.initials: L
authors.lastname: DeLucas
authors.forename: T
authors.initials: T
authors.lastname: Shirasawa
authors.forename: D
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D001923:Brain Chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D005333:Fetus; D006801:Humans; D008969:Molecular Sequence Data; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D011496:Protein Methyltransferases / Q000737:chemistry*
chemical_list: D011496:Protein Methyltransferases; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase