{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,3,25]],"date-time":"2025-03-25T14:46:07Z","timestamp":1742913967966,"version":"3.40.3"},"publisher-location":"New York, NY","reference-count":40,"publisher":"Springer New York","isbn-type":[{"type":"print","value":"9781493922291"},{"type":"electronic","value":"9781493922307"}],"license":[{"start":{"date-parts":[[2014,11,22]],"date-time":"2014-11-22T00:00:00Z","timestamp":1416614400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2014,11,22]],"date-time":"2014-11-22T00:00:00Z","timestamp":1416614400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015]]},"DOI":"10.1007\/978-1-4939-2230-7_12","type":"book-chapter","created":{"date-parts":[[2014,12,10]],"date-time":"2014-12-10T14:15:05Z","timestamp":1418220905000},"page":"211-230","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Methods for the Successful Crystallization of Membrane Proteins"],"prefix":"10.1007","author":[{"given":"Isabel","family":"Moraes","sequence":"first","affiliation":[]},{"given":"Margarida","family":"Archer","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2014,11,22]]},"reference":[{"key":"12_CR1","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1146\/annurev.biophys.33.110502.140348","volume":"33","author":"CR Sanders","year":"2004","unstructured":"Sanders CR, Myers JK (2004) Disease-related misassembly of membrane proteins. Annu Rev Biophys Biomol Struct 33:25\u201351","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"12_CR2","doi-asserted-by":"publisher","first-page":"14371","DOI":"10.1073\/pnas.0804090105","volume":"105","author":"S Wagner","year":"2008","unstructured":"Wagner S, Klepsch MM, Schlegel S et al (2008) Tuning Escherichia coli for membrane protein overexpression. Proc Natl Acad Sci U S A 105:14371\u201314376","journal-title":"Proc Natl Acad Sci U S A"},{"key":"12_CR3","doi-asserted-by":"publisher","first-page":"648","DOI":"10.1016\/j.jmb.2012.07.019","volume":"423","author":"S Schlegel","year":"2012","unstructured":"Schlegel S, L\u00f6fblom J, Lee C et al (2012) Optimizing membrane protein overexpression in the Escherichia coli strain Lemo21 (DE3). J Mol Biol 423:648\u2013659","journal-title":"J Mol Biol"},{"key":"12_CR4","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/S0076-6879(10)70029-X","volume":"470","author":"FA Fays","year":"2010","unstructured":"Fays FA, Zygy R-Z, Stroud RM (2010) Overexpression and purification of integral membrane proteins in yeast. Methods Enzymol 470:695\u2013707","journal-title":"Methods Enzymol"},{"key":"12_CR5","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1038\/nmeth0406-303","volume":"3","author":"D Drew","year":"2006","unstructured":"Drew D, Lerch M, Kunji E et al (2006) Optimization of membrane protein overexpression and purification using GFP fusions. Nat Methods 3:303\u2013313","journal-title":"Nat Methods"},{"key":"12_CR6","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1016\/S0014-5793(01)02711-9","volume":"504","author":"CG Tate","year":"2001","unstructured":"Tate CG (2001) Overexpression of mammalian integral membrane proteins for structural studies. FEBS Lett 504:94\u201398","journal-title":"FEBS Lett"},{"key":"12_CR7","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1016\/j.sbi.2009.07.004","volume":"19","author":"CG Tate","year":"2009","unstructured":"Tate CG, Schertler GF (2009) Engineering G protein-coupled receptors to facilitate their structure determination. Curr Opin Struct Biol 19:386\u2013395","journal-title":"Curr Opin Struct Biol"},{"key":"12_CR8","doi-asserted-by":"publisher","first-page":"967","DOI":"10.1016\/j.str.2012.04.010","volume":"20","author":"E Chun","year":"2012","unstructured":"Chun E, Thompson AA, Liu W et al (2012) Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors. Structure 20:967\u2013976","journal-title":"Structure"},{"key":"12_CR9","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1038\/nature09648","volume":"469","author":"SG Rasmussen","year":"2011","unstructured":"Rasmussen SG, Choi HJ, Fung JJ et al (2011) Structure of a nanobody-stabilized active state of the \u03b22 adrenoceptor. Nature 469:175\u2013180","journal-title":"Nature"},{"key":"12_CR10","doi-asserted-by":"publisher","first-page":"388","DOI":"10.1016\/j.ymeth.2007.01.007","volume":"41","author":"GG Priv\u00e9","year":"2007","unstructured":"Priv\u00e9 GG (2007) Detergents for the stabilization and crystallization of membrane proteins. Methods 41:388\u2013397","journal-title":"Methods"},{"key":"12_CR11","doi-asserted-by":"publisher","first-page":"1003","DOI":"10.1038\/nmeth.1526","volume":"7","author":"PS Chae","year":"2010","unstructured":"Chae PS, Rasmussen SG, Rana RR et al (2010) Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. Nat Methods 7:1003\u20131008","journal-title":"Nat Methods"},{"key":"12_CR12","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1016\/j.bbamem.2011.07.047","volume":"1818","author":"E Serebryany","year":"2012","unstructured":"Serebryany E, Zhu GA, Yan EC (2012) Artificial membrane-like environments for in vitro studies of purified G-protein coupled receptors. Biochim Biophys Acta 1818:225\u2013233","journal-title":"Biochim Biophys Acta"},{"key":"12_CR13","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1107\/S0907444907007652","volume":"63","author":"A D\u2019Arcy","year":"2007","unstructured":"D\u2019Arcy A, Villard F, Marsh M (2007) An automated microseed matrix-screening method for protein crystallization. Acta Crystallogr D Biol Crystallogr 63:550\u2013554","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"12_CR14","doi-asserted-by":"publisher","first-page":"592","DOI":"10.1107\/S0907444912006749","volume":"68","author":"D Axford","year":"2012","unstructured":"Axford D, Owen RL, Foadi J et al (2012) In situ macromolecular crystallography using microbeams. Acta Crystallogr D Biol Crystallogr 68:592\u2013600","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"12_CR15","volume-title":"Protein crystallization strategies for structural genomics","author":"V Cherezov","year":"2007","unstructured":"Cherezov V, Caffrey M (2007) Miniaturization and automation for high-throughput membrane protein crystallization in lipidic mesophases. In: Chayen NE (ed) Protein crystallization strategies for structural genomics. International University Line, San Diego, CA"},{"key":"12_CR16","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.bbamem.2013.07.010","volume":"1838","author":"I Moraes","year":"2014","unstructured":"Moraes I, Evans G, Sanchez-Weatherby J et al (2014) Membrane protein structure determination: the next generation. Biochim Biophys Acta 1838:78\u201387","journal-title":"Biochim Biophys Acta"},{"key":"12_CR17","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1006\/abio.1996.0345","volume":"240","author":"J Wen","year":"1996","unstructured":"Wen J, Arakawa T, Philo JS (1996) Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240:155\u2013166","journal-title":"Anal Biochem"},{"key":"12_CR18","doi-asserted-by":"publisher","first-page":"2207","DOI":"10.1110\/ps.051543805","volume":"14","author":"P Strop","year":"2005","unstructured":"Strop P, Brunger AT (2005) Refractive index-based determination of detergent concentration and its application to the study of membrane proteins. Protein Sci 14:2207\u20132221","journal-title":"Protein Sci"},{"key":"12_CR19","doi-asserted-by":"publisher","first-page":"2309","DOI":"10.1016\/j.bpj.2011.03.004","volume":"100","author":"H Zhao","year":"2011","unstructured":"Zhao H, Brown PH, Schuck P (2011) On the distribution of protein refractive index increments. Biophys J 100:2309\u20132317","journal-title":"Biophys J"},{"key":"12_CR20","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.ymeth.2008.06.012","volume":"46","author":"DJ Slotboom","year":"2008","unstructured":"Slotboom DJ, Duurkens RH, Olieman K, Erkens GB (2008) Static light scattering to characterize membrane proteins in detergent solution. Methods 46:73\u201382","journal-title":"Methods"},{"key":"12_CR21","doi-asserted-by":"publisher","first-page":"10830","DOI":"10.1073\/pnas.0703969104","volume":"104","author":"L Bamber","year":"2007","unstructured":"Bamber L, Harding M, Monn\u00e9 M et al (2007) The yeast mitochondrial ADP\/ATP carrier functions as a monomer in mitochondrial membranes. Proc Natl Acad Sci U S A 104:10830\u201310834","journal-title":"Proc Natl Acad Sci U S A"},{"key":"12_CR22","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1110\/ps.073263108","volume":"17","author":"S Newstead","year":"2008","unstructured":"Newstead S, Ferrandon S, Iwata S (2008) Rationalizing \u03b1-helical membrane protein crystallization. Protein Sci 17:466\u2013472","journal-title":"Protein Sci"},{"key":"12_CR23","doi-asserted-by":"publisher","first-page":"14532","DOI":"10.1073\/pnas.93.25.14532","volume":"93","author":"EM Landau","year":"1996","unstructured":"Landau EM, Rosenbusch JP (1996) Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc Natl Acad Sci U S A 93:14532\u201314535","journal-title":"Proc Natl Acad Sci U S A"},{"key":"12_CR24","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/0304-4157(89)90020-8","volume":"988","author":"G Lindblom","year":"1989","unstructured":"Lindblom G, Rilfors L (1989) Cubic phases and isotropic structures formed by membrane lipids: possible biological relevance. Biochim Biophys Acta 988:221\u2013256","journal-title":"Biochim Biophys Acta"},{"key":"12_CR25","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1107\/S0907444900004716","volume":"56","author":"ML Chiu","year":"2000","unstructured":"Chiu ML, Nollert P, Loewen MEC et al (2000) Crystallization in cubo: general applicability to membrane proteins. Acta Crystallogr D Biol Crystallogr 56:781\u2013784","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"12_CR26","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/S0014-5793(01)02747-8","volume":"504","author":"P Nollert","year":"2001","unstructured":"Nollert P, Qiu H, Caffrey M et al (2001) Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases. FEBS Lett 504:179\u2013186","journal-title":"FEBS Lett"},{"key":"12_CR27","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1038\/368224a0","volume":"368","author":"H Chung","year":"1994","unstructured":"Chung H, Caffrey M (1994) The curvature elastic-energy function of the lipid-water cubic mesophase. Nature 368:224\u2013226","journal-title":"Nature"},{"key":"12_CR28","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1016\/S0006-3495(94)80787-8","volume":"66","author":"H Chung","year":"1994","unstructured":"Chung H, Caffrey M (1994) The neutral area surface of the cubic mesophase: location and properties. Biophys J 66:377\u2013381","journal-title":"Biophys J"},{"key":"12_CR29","doi-asserted-by":"publisher","first-page":"6266","DOI":"10.1021\/bi300010w","volume":"51","author":"M Caffrey","year":"2012","unstructured":"Caffrey M, Li D, Dukkipati A (2012) Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes. Biochemistry 51:6266\u20136288","journal-title":"Biochemistry"},{"key":"12_CR30","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/S0005-2736(97)00047-3","volume":"1327","author":"JM Seddon","year":"1997","unstructured":"Seddon JM, Templer RH, Warrender NA et al (1997) Phosphatidylcholine-fatty acid membranes: effects of headgroup hydration on the phase behaviour and structural parameters of the gel and inverse hexagonal (HII) phases. Biochim Biophys Acta 1327:131\u2013147","journal-title":"Biochim Biophys Acta"},{"key":"12_CR31","doi-asserted-by":"publisher","first-page":"938","DOI":"10.1107\/S0907444998004284","volume":"54","author":"RM Esnouf","year":"1998","unstructured":"Esnouf RM, Ren J, Garman EF et al (1998) Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration. Acta Crystallogr D Biol Crystallogr 54:938\u2013953","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"12_CR32","doi-asserted-by":"publisher","first-page":"1173","DOI":"10.1107\/S0907444905019451","volume":"61","author":"B Heras","year":"2005","unstructured":"Heras B, Martin JL (2005) Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallogr D Biol Crystallogr 61:1173\u20131180","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"12_CR33","doi-asserted-by":"publisher","first-page":"3782","DOI":"10.3390\/ijms13033782","volume":"13","author":"IR Krauss","year":"2012","unstructured":"Krauss IR, Sica F, Mattia CA, Merlino A (2012) Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data. Int J Mol Sci 13:3782\u20133800","journal-title":"Int J Mol Sci"},{"key":"12_CR34","doi-asserted-by":"publisher","first-page":"408","DOI":"10.1038\/nature10450","volume":"478","author":"NJ Hu","year":"2011","unstructured":"Hu NJ, Iwata S, Cameron AD, Drew D (2011) Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature 478:408\u2013411","journal-title":"Nature"},{"key":"12_CR35","doi-asserted-by":"publisher","first-page":"1102","DOI":"10.1038\/ncomms2077","volume":"3","author":"EC McCusker","year":"2012","unstructured":"McCusker EC, Bagn\u00e9ris C, Naylor CE et al (2012) Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing. Nat Commun 3:1102","journal-title":"Nat Commun"},{"key":"12_CR36","doi-asserted-by":"publisher","first-page":"920","DOI":"10.1107\/S0907444913002412","volume":"69","author":"A Douangamath","year":"2013","unstructured":"Douangamath A, Aller P, Lukacik P et al (2013) Using high-throughput in situ plate screening to evaluate the effect of dehydration on protein crystals. Acta Crystallogr D Biol Crystallogr 69:920\u2013923","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"12_CR37","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/0014-5793(91)80217-Q","volume":"280","author":"PA Timmins","year":"1991","unstructured":"Timmins PA, Hauk J, Wacker T, Welte W (1991) The influence of heptane-1, 2, 3-triol on the size and shape of LDAO micelles Implications for the crystallisation of membrane proteins. FEBS Lett 280:115\u2013120","journal-title":"FEBS Lett"},{"key":"12_CR38","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1006\/jmbi.1993.1570","volume":"234","author":"GF Schertler","year":"1993","unstructured":"Schertler GF, Bartunik HD, Michel H, Oesterhelt D (1993) Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 \u00c5 resolution. J Mol Biol 234:156","journal-title":"J Mol Biol"},{"key":"12_CR39","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/0301-4622(94)00073-5","volume":"53","author":"P Timmins","year":"1994","unstructured":"Timmins P, Pebay-Peyroula E, Welte W (1994) Detergent organisation in solutions and in crystals of membrane proteins. Biophys Chem 53:27\u201336","journal-title":"Biophys Chem"},{"key":"12_CR40","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1016\/S0142-9612(99)00126-X","volume":"21","author":"H Qiu","year":"2000","unstructured":"Qiu H, Caffrey M (2000) The phase diagram of the monoolein\/water system: metastability and equilibrium aspects. Biomaterials 21:223\u2013234","journal-title":"Biomaterials"}],"container-title":["Methods in Molecular Biology","Structural Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-4939-2230-7_12","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,20]],"date-time":"2023-01-20T03:37:09Z","timestamp":1674185829000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-1-4939-2230-7_12"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11,22]]},"ISBN":["9781493922291","9781493922307"],"references-count":40,"URL":"https:\/\/doi.org\/10.1007\/978-1-4939-2230-7_12","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"type":"print","value":"1064-3745"},{"type":"electronic","value":"1940-6029"}],"subject":[],"published":{"date-parts":[[2014,11,22]]},"assertion":[{"value":"22 November 2014","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}