Appion: An integrated, database-driven pipeline to facilitate EM image processing

被引:652
作者
Lander, Gabriel C. [1 ]
Stagg, Scott M. [2 ]
Voss, Neil R. [1 ]
Cheng, Anchi [1 ]
Fellmann, Denis [1 ]
Pulokas, James [1 ]
Yoshioka, Craig [1 ]
Irving, Christopher [1 ]
Mulder, Anke [1 ]
Lau, Pick-Wei [1 ]
Lyumkis, Dmitry [1 ]
Potter, Clinton S. [1 ]
Carragher, Bridget [1 ]
机构
[1] Scripps Res Inst, La Jolla, CA 92037 USA
[2] Florida State Univ, Inst Mol Biophys, Dept Chem & Biochem, Tallahassee, FL 32306 USA
基金
美国国家卫生研究院;
关键词
CryoEM; EM; TEM; Single particle analysis; 3D reconstruction; Image processing; Automation; Automated CryoEM; CryoEM pipeline; SINGLE-PARTICLE RECONSTRUCTIONS; ELECTRON CRYOMICROSCOPY; CRYOELECTRON MICROSCOPY; MOLECULAR MICROSCOPY; AUTOMATED CRYOEM; DATA-ACQUISITION; RESOLUTION; SYSTEM; VIRUS; VISUALIZATION;
D O I
10.1016/j.jsb.2009.01.002
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
The use of cryoEM and three-dimensional image reconstruction is becoming increasingly common. Our vision for this technique is to provide a straightforward manner in which users can proceed from raw data to a reliable 3D reconstruction through a pipeline that both facilitates management of the processing steps and makes the results at each step more transparent. Tightly integrated with a relational SQL database, Appion is a modular and transparent pipeline that extends existing software applications and procedures. The user manages and controls the software modules via web-based forms, and all results are similarly available using web-based viewers directly linked to the underlying database, enabling even naive users to quickly deduce the quality of their results. The Appion API was designed with the principle that applications should be compatible with a broad range of specimens and that libraries and routines are modular and extensible. Presented here is a description of the design and architecture of the working Appion pipeline prototype and some results of its use. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:95 / 102
页数:8
相关论文
共 27 条
[1]   Determination of the fold of the core protein of hepatitis B virus ky electron cryomicroscopy [J].
Bottcher, B ;
Wynne, SA ;
Crowther, RA .
NATURE, 1997, 386 (6620) :88-91
[2]   Does contamination buildup limit throughput for automated cryoEM? [J].
Cheng, AC ;
Fellmann, D ;
Pulokas, J ;
Potter, CS ;
Carragher, B .
JOURNAL OF STRUCTURAL BIOLOGY, 2006, 154 (03) :303-311
[3]   Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy [J].
Conway, JF ;
Cheng, N ;
Zlotnick, A ;
Wingfield, PT ;
Stahl, SJ ;
Steven, AC .
NATURE, 1997, 386 (6620) :91-94
[4]   A relational database for cryoEM: experience at one year and 50 000 images [J].
Fellmann, D ;
Pulokas, J ;
Milligan, RA ;
Carragher, B ;
Potter, CS .
JOURNAL OF STRUCTURAL BIOLOGY, 2002, 137 (03) :273-282
[5]   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
[6]   FREALIGN: High-resolution refinement of single particle structures [J].
Grigorieff, Nikolaus .
JOURNAL OF STRUCTURAL BIOLOGY, 2007, 157 (01) :117-125
[7]  
HARAUZ G, 1986, OPTIK, V73, P146
[8]   SPARX, a new environment for Cryo-EM image processing [J].
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. .
JOURNAL OF STRUCTURAL BIOLOGY, 2007, 157 (01) :47-55
[9]   Backbone structure of the infectious ε15 virus capsid revealed by electron cryomicroscopy [J].
Jiang, Wen ;
Baker, Matthew L. ;
Jakana, Joanita ;
Weigele, Peter R. ;
King, Jonathan ;
Chiu, Wah .
NATURE, 2008, 451 (7182) :1130-U12
[10]   Bacteriophage lambda stabilization by auxiliary protein gpD: Timing, location, and mechanism of attachment determined by cryo-EM [J].
Lander, Gabriel C. ;
Evilevitch, Alex ;
Jeembaeva, Meerim ;
Potter, Clinton S. ;
Carragher, Bridget ;
Johnson, John E. .
STRUCTURE, 2008, 16 (09) :1399-1406