title: Crystallization and preliminary X-ray investigation of a ubiquitin carrier protein (E2) from Arabidopsis thaliana.
abstract: Crystals of a recombinant ubiquitin carrier protein from Arabidopsis thaliana have been grown from solutions of ammonium sulfate. The crystals are orthorhombic, space group P2(1)2(1)2(1); the axes are a = 41.8(1) A, b = 44.9(1) A and c = 83.2(1) A. The crystals are quite stable to X-rays and diffract beyond 2.1 A resolution. There is one molecule in the asymmetric unit.
authors.affiliation: Department of Pathology, University of Alabama, Birmingham 35294.
authors.forename: W J
authors.initials: WJ
authors.lastname: Cook
authors.forename: L C
authors.initials: LC
authors.lastname: Jeffrey
authors.forename: M L
authors.initials: ML
authors.lastname: Sullivan
authors.forename: R D
authors.initials: RD
authors.lastname: Vierstra
mesh_terms: D002352:Carrier Proteins / Q000648:ultrastructure*; D003461:Crystallography; D008025:Ligases; D010940:Plant Proteins / Q000648:ultrastructure*; D010944:Plants; D011994:Recombinant Proteins / Q000648:ultrastructure; D044763:Ubiquitin-Conjugating Enzymes; D014452:Ubiquitins / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D002352:Carrier Proteins; D010940:Plant Proteins; D011994:Recombinant Proteins; D014452:Ubiquitins; C046288:ubiquitin carrier proteins; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases