Crystallization and initial X-ray diffraction analysis of human pyruvate dehydrogenase.
Crystallization and initial X-ray diffraction analysis of human pyruvate dehydrogenase.
复制标题
人丙酮酸脱氢酶的结晶和初始 X 射线衍射分析。
DOI:
10.1107/s0907444901000427
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发表时间:
2001
期刊:
影响因子:
--
通讯作者:
Patel,MS
中科院分区:
文献类型:
--
作者:
Ciszak,E;Korotchkina,LG;Hong,YS;Joachimiak,A;Patel,MS
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 α2β2 tetramer (∼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 P212121, with unit-cell parameters a = 64.2, b = 126.9, c = 190.2 Å. Crystals diffracted to a minimum d spacing of 2.5 Å. The asymmetric unit contains one α2β2 tetrameric E1 assembly; self-rotation function analysis showed a pseudo-twofold symmetry relating the two αβ dimers.
DOI:
10.1016/0006-291x(77)90636-2
发表时间:
1977
影响因子:
3.1
作者:
James R. Butler;F. Pettit;P. Davis;Lester J. Reed
通讯作者:
Lester J. Reed
DOI:
10.1042/bj1730659
发表时间:
1978
期刊:
The Biochemical journal
影响因子:
--
作者:
P. Sugden;P. J. Randle
通讯作者:
P. J. Randle