Artículos de revistas
Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM)
Registro en:
Acta Crystallographica Section D-biological Crystallography. Munksgaard Int Publ Ltd, v. 56, n. 1492, n. 1494, 2000.
0907-4449
WOS:000165336100032
10.1107/S0907444900011380
Autor
Aparicio, R
Ferreira, ST
Leite, NR
Polikarpov, I
Institución
Resumen
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 Angstrom and diffracted to 2.25 Angstrom at 85 K, whereas form B had unit-cell parameters a = 73.02, b = 79.80, c = 172.85 Angstrom and diffracted to 2.85 Angstrom 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. 56 11 1492 1494