Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction.
Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction.
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通过冷冻电子显微镜和 X 射线衍射对原肌球蛋白进行结构研究。
DOI:
10.1016/s0006-3495(91)82293-7
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发表时间:
1991
影响因子:
3.4
通讯作者:
Cohen,C
中科院分区:
文献类型:
--
作者:
Cabral-Lilly,D;PhillipsJr,GN;Sosinsky,GE;Melanson,L;Chacko,S;Cohen,C
A comparison has been made between cryoelectron microscope images and the x-ray structure of one projection of the Bailey tropomyosin crystal. The computed transforms of the electron micrographs extend to a resolution of approximately 18 A compared with the reflections from x-ray crystallography which extend to 15 A. After correction of the images for lattice distortions and the contrast transfer function, the structure factors were constrained to the plane group (pmg) symmetry of this projection. Amplitude and phase data for five images were compared with the corresponding view from the three-dimensional x-ray diffraction data (Phillips, G.N., Jr., J.P. Fillers, and C. Cohen. 1986. J. Mol. Biol. 192: 111–131). The average R factor between the electron microscopy and x-ray amplitudes was 15%, with an amplitude-weighted mean phase difference of 4.8 degrees. The density maps derived from cryoelectron microscopy contain structural features similar to those from x-ray diffraction: these include the width and run of the filaments and their woven appearance at the crossover regions. Preliminary images obtained from frozen-hydrated tropomyosin/troponin cocrystals suggest that this approach may provide structural details not readily obtainable from x-ray diffraction studies.
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影响因子:
5.6
作者:
PhillipsJr,GN;Cohen,C;Stewart,M
通讯作者:
Stewart,M
影响因子:
5.6
作者:
S. Higashi;T. Ooi
通讯作者:
T. Ooi
影响因子:
3.4
作者:
Sosinsky,GE;Baker,TS;Caspar,DL;Goodenough,DA
通讯作者:
Goodenough,DA
影响因子:
5.6
作者:
CASPAR, DLD;COHEN, C;LONGLEY, W
通讯作者:
LONGLEY, W
影响因子:
5.6
作者:
PHILLIPS, GN;FILLERS, JP;COHEN, C
通讯作者:
COHEN, C