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|Type:||Artigo de periódico|
|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 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.|
|Editor:||Munksgaard Int Publ Ltd|
|Citation:||Acta Crystallographica Section D-biological Crystallography. Munksgaard Int Publ Ltd, v. 56, n. 1492, n. 1494, 2000.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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