<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adiga, Umesh</style></author><author><style face="normal" font="default" size="100%">Baxter, Bill</style></author><author><style face="normal" font="default" size="100%">Hall, Richard J</style></author><author><style face="normal" font="default" size="100%">Rockel, Beate</style></author><author><style face="normal" font="default" size="100%">Rath, Bimal K</style></author><author><style face="normal" font="default" size="100%">Frank, Joachim</style></author><author><style face="normal" font="default" size="100%">Glaeser, Robert M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Particle picking by segmentation: a comparative study with SPIDER-based manual particle picking.</style></title><secondary-title><style face="normal" font="default" size="100%">J Struct Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Struct. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Algorithms</style></keyword><keyword><style  face="normal" font="default" size="100%">Aminopeptidases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryoelectron Microscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</style></keyword><keyword><style  face="normal" font="default" size="100%">Image Processing, Computer-Assisted</style></keyword><keyword><style  face="normal" font="default" size="100%">Imaging, Three-Dimensional</style></keyword><keyword><style  face="normal" font="default" size="100%">Internet</style></keyword><keyword><style  face="normal" font="default" size="100%">Particle Size</style></keyword><keyword><style  face="normal" font="default" size="100%">Ribosomes</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine Endopeptidases</style></keyword><keyword><style  face="normal" font="default" size="100%">Software</style></keyword><keyword><style  face="normal" font="default" size="100%">Software Validation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">12/2005</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16330229</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">152</style></volume><pages><style face="normal" font="default" size="100%">211-20</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;span style=&quot;font-family: arial, helvetica, clean, sans-serif; font-size: 13px; line-height: 17px;&quot;&gt;Boxing hundreds of thousands of particles in low-dose electron micrographs is one of the major bottle-necks in advancing toward achieving atomic resolution reconstructions of biological macromolecules. We have shown that a combination of pre-processing operations and segmentation can be used as an effective, automatic tool for identifying and boxing single-particle images. This paper provides a brief description of how this method has been applied to a large data set of micrographs of ice-embedded ribosomes, including a comparative analysis of the efficiency of the method. Some results on processing micrographs of tripeptidyl peptidase II particles are also shown. In both cases, we have achieved our goal of selecting at least 80% of the particles that an expert would select with less than 10% false positives.&lt;/span&gt;&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue></record></records></xml>