Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM).
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.
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Laboratório Nacional de Luz Síncrotron (LNLS), Caixa Postal 6192, CEP 13083-970, Brazil, and Instituto de Física Gleb Wataghin, UNICAMP, Brazil.
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Polikarpov
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D000818:Animals; D018360:Crystallography, X-Ray; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D011817:Rabbits; D014305:Triose-Phosphate Isomerase / Q000737:chemistry*
D014305:Triose-Phosphate Isomerase