title: Crystallization and preliminary X-ray diffraction studies of the ubiquitin-like (UbL) domain of the human homologue A of Rad23 (hHR23A) protein.
abstract: Human homologue A of Rad23 (hHR23A) plays dual roles in DNA repair as well as serving as a shuttle vehicle targeting polyubiquitinated proteins for degradation. Its N-terminal ubiquitin-like (UbL) domain interacts with the 19S proteasomal cap and provides the docking mechanism for protein delivery. Pyramidal crystals of the UbL domain of hHR23A were obtained by the hanging-drop vapour-diffusion method with ammonium sulfate as the crystallizing agent. The crystals diffracted to beyond 2 A resolution and belonged to the hexagonal space group P6(5)22, with unit-cell parameters a = b = 78.48, c = 63.57 A. The structure was solved by molecular replacement using the UbL domain of yeast Dsk2 as the search model.
authors.affiliation: Randall Division of Cell and Molecular Biophysics, King's College London, London, England. yu-wai.chen@kcl.ac.uk
authors.forename: Yu Wai
authors.initials: YW
authors.lastname: Chen
authors.forename: Toshitaka
authors.initials: T
authors.lastname: Tajima
authors.forename: Martin
authors.initials: M
authors.lastname: Rees
authors.forename: Mitla
authors.initials: M
authors.lastname: Garcia-Maya
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D045643:DNA Repair Enzymes / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D004268:DNA-Binding Proteins; D025801:Ubiquitin; C086985:RAD23A protein, human; D045643:DNA Repair Enzymes