title: Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM).
abstract: Triose phosphate isomerase (TIM) is responsible for the interconversion between GAP and DHAP in the glycolytic pathway. Two crystal forms belonging to space group P2(1)2(1)2(1) were obtained by the hanging-drop method and were designated A and B. Synchrotron X-ray diffraction data were collected for both forms. Form A had unit-cell parameters a = 65.14, b = 72.45, c = 93.24 A and diffracted to 2.25 A at 85 K, whereas form B had unit-cell parameters a = 73.02, b = 79.80, c = 172.85 A and diffracted to 2.85 A at room temperature. Molecular replacement was employed to solve the structures, using human TIM as a search model. Further refinement of both structures is under way and is expected to shed light on the recently reported conformational studies for rabbit TIM.
authors.affiliation: Laboratório Nacional de Luz Síncrotron (LNLS), Caixa Postal 6192, CEP 13083-970, Brazil, and Instituto de Física Gleb Wataghin, UNICAMP, Brazil.
authors.forename: R
authors.initials: R
authors.lastname: Aparicio
authors.forename: S T
authors.initials: ST
authors.lastname: Ferreira
authors.forename: N R
authors.initials: NR
authors.lastname: Leite
authors.forename: I
authors.initials: I
authors.lastname: Polikarpov
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D011817:Rabbits; D014305:Triose-Phosphate Isomerase / Q000737:chemistry*
chemical_list: D014305:Triose-Phosphate Isomerase