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| Crystallization and initial X-ray diffraction analysis of human pyruvate dehydrogenase. E Ciszak , L G Korotchkina , Y S Hong , A Joachimiak , M S Patel Acta Cryst. D 2001; 57 465-468 ICID: 550801 | ||
| Article type: Original article | ||
| IC™ Value: 13.07 | ||
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| Human pyruvate dehydrogenase (E1) is a component enzyme of the pyruvate dehydrogenase complex. The enzyme catalyzes the irreversible decarboxylation of pyruvic acid and the rate-limiting reductive acetylation of the lipoyl moiety linked to the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex. E1 is an alpha(2)beta(2) tetramer ( approximately 154 kDa). Crystals of this recombinant enzyme have been grown in polyethylene glycol 3350 using a vapor-diffusion method at 295 K. The crystals are characterized as orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 64.2, b = 126.9, c = 190.2 A. Crystals diffracted to a minimum d spacing of 2.5 A. The asymmetric unit contains one alpha(2)beta(2) tetrameric E1 assembly; self-rotation function analysis showed a pseudo-twofold symmetry relating the two alphabeta dimers. | ||
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ICID 550801 PMID 11223534 - click here to show this article in PubMed database | ||
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