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First, a tissue sample or cell pellet is obtained. The cells are isolated, washed, and then lysed either by sonication, bead beating, or manual homogenization. Membrane proteins are fractionated from the lysates by centrifugation and solubilized in a mild detergent suitable for crystallization, such as <jats:italic>n<\/jats:italic>\u2010dodecyl\u2010\u03b2\u2010maltoside (DDM). Detergent extracts are then centrifuged, heat precipitated, and filtered to remove insoluble, thermally unstable, and\/or aggregated proteins. Samples are then prepared for analysis by mass spectrometry: proteins are precipitated by methanol\/chloroform extraction and subjected to reduction, alkylation, and protease digestion. The resulting peptides are passed through a detergent removal column, desalted, rehydrated in 0.1% formic acid (v\/v), and identified by LC\u2010MS\/MS. \u00a9 2017 by John Wiley &amp; Sons, Inc.<\/jats:p>","DOI":"10.1002\/cpps.40","type":"journal-article","created":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T14:13:04Z","timestamp":1509545584000},"source":"Crossref","is-referenced-by-count":0,"title":["Screening and Identifying Membrane Proteins Favorable for Crystallization"],"prefix":"10.1002","volume":"90","author":[{"given":"Jared","family":"Kim","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Hawaii at Manoa  Honolulu Hawaii"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ho Leung","family":"Ng","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University  Manhattan Kansas"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2018,2,13]]},"reference":[{"key":"e_1_2_4_2_1_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.sbi.2008.07.001"},{"key":"e_1_2_4_2_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr800308v"},{"key":"e_1_2_4_2_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2012.06.009"},{"key":"e_1_2_4_2_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.2766"},{"key":"e_1_2_4_2_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2008.11.021"},{"key":"e_1_2_4_2_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/nprot.2009.27"},{"key":"e_1_2_4_2_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ymeth.2007.01.007"},{"key":"e_1_2_4_2_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr0602491"},{"key":"e_1_2_4_2_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/80691"},{"key":"e_1_2_4_2_10_1","doi-asserted-by":"publisher","DOI":"10.1110\/ps.073037907"},{"key":"e_1_2_4_2_11_1","first-page":"29.11:29.11.1","article-title":"General qPCR and plate reader methods for rapid optimization of membrane protein purification and crystallization using thermostability assays","volume":"77","author":"Tomasiak T. 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