MonoRes: Automatic and Accurate Estimation of Local Resolution for Electron Microscopy Maps

被引:143
作者
Luis Vilas, Jose [1 ]
Gomez-Blanco, Josue [1 ]
Conesa, Pablo [1 ]
Melero, Roberto [1 ]
iguel de la Rosa-Trevin, Jose [2 ]
Oton, Joaquin [1 ]
Cuenca, Jesus [1 ]
Marabini, Roberto [3 ]
Maria Carazo, Jose [1 ]
Vargas, Javier [4 ]
Sorzano, Carlos Oscar S. [1 ,5 ]
机构
[1] CSIC, Natl Ctr Biotechnol, Biocomp Unit, Darwin 3,Campus Univ Autonoma, E-28049 Madrid, Spain
[2] Stockholm Univ, Sci Life Lab, Stockholm, Sweden
[3] Univ Autonoma Madrid, Escuela Politecn Super, E-28049 Madrid, Spain
[4] McGill Univ, Dept Anat & Cell Biol, Univ St Strathcona Anat Bldg 3640, Montreal, PQ, Canada
[5] Univ San Pablo CEU, Dept Engn Elect & Telecommun Syst, Campus Urbanizac Monteprincipe, Madrid 28668, Spain
关键词
CRYO-EM STRUCTURE; SIGNAL; TRANSFORM; RECONSTRUCTIONS; DEMODULATION;
D O I
10.1016/j.str.2017.12.018
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Since the beginning of electron microscopy, resolution has been a critical parameter. In this article, we propose a fully automatic, accurate method for determining the local resolution of a 3D map (MonoRes). The foundation of this algorithm is an extension of the concept of analytic signal, termed monogenic signal. The map is filtered at different frequencies and the amplitude of the monogenic signal is calculated, after which a criterion is applied to determine the resolution at each voxel. MonoRes is fully automatic without compulsory user parameters, with great accuracy in all tests, and is computationally more rapid than existing methods in the field. In addition, MonoRes offers the option of local filtering of the original map based on the calculated local resolution.
引用
收藏
页码:337 / +
页数:12
相关论文
共 31 条
[1]   2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor [J].
Bartesaghi, Alberto ;
Merk, Alan ;
Banerjee, Soojay ;
Matthies, Doreen ;
Wu, Xiongwu ;
Milne, Jacqueline L. S. ;
Subramaniam, Sriram .
SCIENCE, 2015, 348 (6239) :1147-1151
[2]   2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy [J].
Campbell, Melody G. ;
Veesler, David ;
Cheng, Anchi ;
Potter, Clinton S. ;
Carragher, Bridget .
ELIFE, 2015, 4 :1-22
[3]   One number does not fit all: Mapping local variations in resolution in cryo-EM reconstructions [J].
Cardone, Giovanni ;
Heymann, J. Bernard ;
Steven, Alasdair C. .
JOURNAL OF STRUCTURAL BIOLOGY, 2013, 184 (02) :226-236
[4]   Architecture of the type IVa pilus machine [J].
Chang, Yi-Wei ;
Rettberg, Lee A. ;
Treuner-Lange, Anke ;
Iwasa, Janet ;
Sogaard-Andersen, Lotte ;
Jensen, Grant J. .
SCIENCE, 2016, 351 (6278)
[5]  
Conesa P., 2017, PROTEIN SCI, V27, P269
[6]   Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy [J].
de la Rosa-Trevin, J. M. ;
Quintana, A. ;
del Cano, L. ;
Zaldivar, A. ;
Foche, I. ;
Gutierrez, J. ;
Gomez-Blanco, J. ;
Burguet-Castell, J. ;
Cuenca-Alba, J. ;
Abrishami, V. ;
Vargas, J. ;
Oton, J. ;
Sharov, G. ;
Vilas, J. L. ;
Navas, J. ;
Conesa, P. ;
Kazemi, M. ;
Marabini, R. ;
Sorzano, C. O. S. ;
Carazo, J. M. .
JOURNAL OF STRUCTURAL BIOLOGY, 2016, 195 (01) :93-99
[7]   Xmipp 3.0: An improved software suite for image processing in electron microscopy [J].
de la Rosa-Trevin, J. M. ;
Oton, J. ;
Marabini, R. ;
Zaldivar, A. ;
Vargas, J. ;
Carazo, J. M. ;
Sorzano, C. O. S. .
JOURNAL OF STRUCTURAL BIOLOGY, 2013, 184 (02) :321-328
[8]   The monogenic signal [J].
Felsberg, M ;
Sommer, G .
IEEE TRANSACTIONS ON SIGNAL PROCESSING, 2001, 49 (12) :3136-3144
[9]  
Gabor D, 1946, J. Inst. Electr. Eng. (London), V93, P429, DOI [10.1049/JI-3-2.1946.0074, DOI 10.1049/JI-3-2.1946.0074, 10.1049/ji-3-2.1946.0074]
[10]  
HARAUZ G, 1986, OPTIK, V73, P146