Automatic lattice determination for two-dimensional crystal images.
Electron crystallography determines the structure of membrane proteins and other periodic samples by recording either images or diffraction patterns. Computer processing of recorded images requires the determination of the reciprocal lattice parameters in the Fourier transform of the image. We have developed a set of three programs 2dx_peaksearch, 2dx_findlat and 2dx_getlat, which can determine the reciprocal lattice from a Fourier transformation of a 2D crystal image automatically. 2dx_peaksearch determines a list of Fourier peak coordinates from a processed calculated diffraction pattern. These coordinates are evaluated by 2dx_findlat to determine one or more lattices, using a-priori knowledge of the real-space crystal unit cell dimensions, and the sample tilt geometry. If these are unknown, then the program 2dx_getlat can be used to obtain a guess for the unit cell dimensions. These programs are available as part of the 2dx software package for the image processing of 2D crystal images at http://2dx.org.
Zeng
Xiangyan
X
Molecular & Cellular Biology, Briggs Hall, College of Biological Sciences, University of California at Davis, 1 Shields Ave., Davis, CA 95616, USA.
Gipson
Bryant
B
Zheng
Zi Yan
ZY
Renault
Ludovic
L
Stahlberg
Henning
H
D000465:Algorithms; D003460:Crystallization; D003461:Crystallography / Q000379:methods*; D005583:Fourier Analysis; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry / Q000648:ultrastructure*; D046529:Microscopy, Electron, Transmission / Q000379:methods*; D012984:Software
D008565:Membrane Proteins