| Autor: |
Aparicio R; Laboratório Nacional de Luz Síncrotron (LNLS), Caixa Postal 6192, CEP 13083-970, Brazil, and Instituto de Física Gleb Wataghin, UNICAMP, Brazil., Ferreira ST, Leite NR, Polikarpov I |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2000 Nov; Vol. 56 (Pt 11), pp. 1492-4. |
| DOI: |
10.1107/s0907444900011380 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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