SPARX, a new environment for Cryo-EM image processing

被引:294
作者
Hohn, Michael
Tang, Grant
Goodyear, Grant
Baldwin, P. R.
Huang, Zhong
Penczek, Pawel A.
Yang, Chao
Glaeser, Robert M.
Adams, Paul D.
Ludtke, Steven J. [1 ]
机构
[1] Baylor Coll Med, Natl Ctr Macromol Imaging, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA
[2] Lawrence Berkeley Natl Lab, Phys Biosci Div, Berkeley, CA 94720 USA
[3] Univ Texas, Houston Med Ctr, Dept Biochem & Mol Biol, Houston, TX 77030 USA
[4] Univ Calif Berkeley, Dept Mol & Cell Biol, Phys Biosci Div, Lawrence Berkeley Natl Lab, Berkeley, CA 94720 USA
[5] Lawrence Berkeley Natl Lab, Berkeley, CA 94720 USA
关键词
CryoEM; TEM; single particle analysis; 3-D reconstruction; image processing;
D O I
10.1016/j.jsb.2006.07.003
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
SPARX (single particle analysis for resolution extension) is a new image processing environment with a particular emphasis on transmission electron microscopy (TEM) Structure determination. It includes a graphical User interface that provides a complete graphical programming environment with a novel data/process-flow infrastructure, an extensive library of Python scripts that perform specific TEM-related computational tasks, and a core library of fundamental C++ image processing functions. In addition, SPARX relies on the EMAN2 library and cctbx, the open-source computational crystallography library from PHENIX. The design of the system is Such that future inclusion of other image processing libraries is a straightforward task. The SPARX infrastructure intelligently handles retention of intermediate values, even those inside programming Structures Such as loops and function calls. SPARX and all dependencies are free for academic use and available with complete source. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:47 / 55
页数:9
相关论文
共 24 条
[1]  
Abrahams D., 2003, C/C++ Users Journal, V21, P29
[2]   Recent developments in the PHENIX software for automated crystallographic structure determination [J].
Adams, PD ;
Gopal, K ;
Grosse-Kunstleve, RW ;
Hung, LW ;
Ioerger, TR ;
McCoy, AJ ;
Moriarty, NW ;
Pai, RK ;
Read, RJ ;
Romo, TD ;
Sacchettin, JC ;
Sauter, NK ;
Storoni, LC ;
Terwilligerf, TC .
JOURNAL OF SYNCHROTRON RADIATION, 2004, 11 :53-55
[3]   PHENIX:: building new software for automated crystallographic structure determination [J].
Adams, PD ;
Grosse-Kunstleve, RW ;
Hung, LW ;
Ioerger, TR ;
McCoy, AJ ;
Moriarty, NW ;
Read, RJ ;
Sacchettini, JC ;
Sauter, NK ;
Terwilliger, TC .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2002, 58 :1948-1954
[4]   A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy [J].
Baker, TS ;
Cheng, RH .
JOURNAL OF STRUCTURAL BIOLOGY, 1996, 116 (01) :120-130
[5]   Helical processing using PHOELIX [J].
Carragher, B ;
Whittaker, M ;
Milligan, RA .
JOURNAL OF STRUCTURAL BIOLOGY, 1996, 116 (01) :107-112
[6]   MRC image processing programs [J].
Crowther, RA ;
Henderson, R ;
Smith, JM .
JOURNAL OF STRUCTURAL BIOLOGY, 1996, 116 (01) :9-16
[7]   SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields [J].
Frank, J ;
Radermacher, M ;
Penczek, P ;
Zhu, J ;
Li, YH ;
Ladjadj, M ;
Leith, A .
JOURNAL OF STRUCTURAL BIOLOGY, 1996, 116 (01) :190-199
[8]   ALGEBRAIC RECONSTRUCTION TECHNIQUES (ART) FOR 3-DIMENSIONAL ELECTRON MICROSCOPY AND X-RAY PHOTOGRAPHY [J].
GORDON, R ;
BENDER, R ;
HERMAN, GT .
JOURNAL OF THEORETICAL BIOLOGY, 1970, 29 (03) :471-&
[9]   Three-dimensional structure of bovine NADH:Ubiquinone oxidoreductase (Complex I) at 22 Å in ice [J].
Grigorieff, N .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 277 (05) :1033-1046
[10]   The Computational Crystallography Toolbox:: crystallographic algorithms in a reusable software framework [J].
Grosse-Kunstleve, RW ;
Sauter, NK ;
Moriarty, NW ;
Adams, PD .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 2002, 35 :126-136