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
Cohen,C
中科院分区:
生物学3区
文献类型:
--
作者:
Cabral-Lilly,D;PhillipsJr,GN;Sosinsky,GE;Melanson,L;Chacko,S;Cohen,C

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一个比较已之间的冷冻电子显微镜图像和贝利原肌球蛋白晶体的一个投影的X-射线结构。电子显微照片的计算变换延伸到大约18 A的分辨率,与之相比,从X射线晶体学延伸到15 A的反射。在对晶格畸变和对比度传递函数的图像进行校正之后,结构因子被约束到该投影的平面群(pmg)对称性。将五幅图像的振幅和相位数据与来自三维X射线衍射数据的相应视图进行比较(菲利普斯,G.N.,小的,J.P. Fillers和C.科恩1986. J. Mol. 192:111-131)。电子显微镜和X射线振幅之间的平均R因子为15%,振幅加权平均相位差为4.8度。来自低温电子显微镜的密度图包含类似于来自X射线衍射的结构特征:这些包括长丝的宽度和运行以及它们在交叉区域的编织外观。从冷冻水合原肌球蛋白/肌钙蛋白共晶体获得的初步图像表明,这种方法可以提供不容易从X射线衍射研究获得的结构细节。
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.
DOI: 10.1016/0022-2836(87)90339-1
发表时间: 1987
影响因子: 5.6
作者:
PhillipsJr,GN;Cohen,C;Stewart,M
通讯作者: Stewart,M
原肌球蛋白和天然原肌球蛋白的晶体。
DOI: 10.1016/0022-2836(68)90190-3
发表时间: 1968
影响因子: 5.6
作者:
S. Higashi;T. Ooi
通讯作者: T. Ooi
间隙连接晶格图像的相关分析。
DOI: 10.1016/s0006-3495(90)82462-0
发表时间: 1990
影响因子: 3.4
作者:
Sosinsky,GE;Baker,TS;Caspar,DL;Goodenough,DA
通讯作者: Goodenough,DA
DOI: 10.1016/0022-2836(69)90128-4
发表时间: 1969-01-01
影响因子: 5.6
作者:
CASPAR, DLD;COHEN, C;LONGLEY, W
通讯作者: LONGLEY, W
DOI: 10.1016/0022-2836(86)90468-7
发表时间: 1986-11-05
影响因子: 5.6
作者:
PHILLIPS, GN;FILLERS, JP;COHEN, C
通讯作者: COHEN, C