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Volumn 374, Issue 2072, 2016, Pages

Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironment during the growth of single transmembrane α-helical peptide crystals

Author keywords

Cubic mesophase; DAP12; In meso crystallization; Local lamellar phase

Indexed keywords

CRYSTAL GROWTH; LAMELLAR STRUCTURES; PEPTIDES; PROTEINS; X RAY CRYSTALLOGRAPHY; X RAY SCATTERING;

EID: 84974845852     PISSN: 1364503X     EISSN: None     Source Type: Journal    
DOI: 10.1098/rsta.2015.0125     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau EM, Rosenbusch JP. 1996 Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA 93, 14 532-14 535. (doi:10.1073/pnas.93. 25.14532)
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 2
    • 4043142190 scopus 로고    scopus 로고
    • Structural genomics on membrane proteins: The MePNet approach
    • Lundstrom K. 2004 Structural genomics on membrane proteins: the MePNet approach. Curr. Opin. Drug Discov. Dev. 7, 342-346.
    • (2004) Curr. Opin. Drug Discov. Dev. , vol.7 , pp. 342-346
    • Lundstrom, K.1
  • 3
    • 84896798303 scopus 로고    scopus 로고
    • Gently does it
    • Service RF. 2014 Gently does it. Science 343, 1094-1097. (doi:10.1126/science.343.6175.1094)
    • (2014) Science , vol.343 , pp. 1094-1097
    • Service, R.F.1
  • 4
    • 80052089906 scopus 로고    scopus 로고
    • Lipidic cubic phase technologies for membrane protein structural studies
    • Cherezov V. 2011 Lipidic cubic phase technologies for membrane protein structural studies. Curr. Opin. Struct. Biol. 21, 559-566. (doi:10.1016/j.sbi.2011.06.007)
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 559-566
    • Cherezov, V.1
  • 5
    • 84865138166 scopus 로고    scopus 로고
    • Membrane protein structure determination using crystallography and lipidic mesophases: Recent advances and successes
    • Caffrey M, Li DF, Dukkipati A. 2012 Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes. Biochemistry 51, 6266-6288. (doi:10.1021/Bi300010w)
    • (2012) Biochemistry , vol.51 , pp. 6266-6288
    • Caffrey, M.1    Li, D.F.2    Dukkipati, A.3
  • 6
    • 84897500205 scopus 로고    scopus 로고
    • Crystallizing membrane proteins in the lipidic mesophase. Experience with human prostaglandin E2 synthase 1 and an evolving strategy
    • Li D et al. 2014 Crystallizing membrane proteins in the lipidic mesophase. Experience with human prostaglandin E2 synthase 1 and an evolving strategy. Cryst. Growth Des. 14, 2034-2047. (doi:10.1021/cg500157x)
    • (2014) Cryst. Growth Des. , vol.14 , pp. 2034-2047
    • Li, D.1
  • 7
    • 84921728247 scopus 로고    scopus 로고
    • A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes
    • Caffrey M. 2015 A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes. Acta Crystallogr. Sect. F Struct. Biol. Commun. 71, 3-18. (doi:10.1107/S2053230X14026843)
    • (2015) Acta Crystallogr. Sect. F Struct. Biol. Commun. , vol.71 , pp. 3-18
    • Caffrey, M.1
  • 8
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G. 1998 Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7, 1029-1038. (doi:10.1002/pro. 5560070420)
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 9
    • 75949095090 scopus 로고    scopus 로고
    • Membrane protein structures
    • Doerr A. 2009 Membrane protein structures. Nat. Methods. 6, 35. (doi:10.1038/Nmeth.F.240)
    • (2009) Nat. Methods. , vol.6 , pp. 35
    • Doerr, A.1
  • 10
    • 84890840505 scopus 로고    scopus 로고
    • Serial femtosecond crystallography of G protein-coupled receptors
    • Liu W et al. 2013 Serial femtosecond crystallography of G protein-coupled receptors. Science 342, 1521-1524. (doi:10.1126/science.1244142)
    • (2013) Science , vol.342 , pp. 1521-1524
    • Liu, W.1
  • 11
    • 84894037590 scopus 로고    scopus 로고
    • Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography
    • Weierstall U et al. 2014 Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography. Nat. Commun. 5, 3309. (doi:10.1038/Ncomms4309)
    • (2014) Nat. Commun. , vol.5 , pp. 3309
    • Weierstall, U.1
  • 12
    • 84879867305 scopus 로고    scopus 로고
    • Host lipid and temperature as important screening variables for crystallizing integral membrane proteins in lipidic mesophases
    • Li DF, Shah STA, Caffrey M. 2013 Host lipid and temperature as important screening variables for crystallizing integral membrane proteins in lipidic mesophases. Trials with diacylglycerol kinase. Cryst. Growth Des. 13, 2846-2857. (doi:10.1021/Cg400254v)
    • (2013) Trials with diacylglycerol kinase. Cryst. Growth Des. , vol.13 , pp. 2846-2857
    • Li, D.F.1    Shah, S.T.A.2    Caffrey, M.3
  • 13
    • 34547803687 scopus 로고    scopus 로고
    • Membrane protein crystallization in lipidic mesophases. A mechanism study using X-ray microdiffraction
    • Cherezov V, Caffrey M. 2007 Membrane protein crystallization in lipidic mesophases. A mechanism study using X-ray microdiffraction.Faraday Discuss. 136, 195-212. (doi:10.1039/ B618173b)
    • (2007) Faraday Discuss , vol.136 , pp. 195-212
    • Cherezov, V.1    Caffrey, M.2
  • 14
    • 0141817680 scopus 로고    scopus 로고
    • Electron microscopic evidence for nucleation and growth of 3D acetylcholine receptor microcrystals in structured lipid-detergent matrices
    • Paas Y, Cartaud J, Recouvreur M, Grailhe R, Dufresne V, Pebay-Peyroula E, Landau EM, Changeux JP. 2003 Electron microscopic evidence for nucleation and growth of 3D acetylcholine receptor microcrystals in structured lipid-detergent matrices. Proc. Natl Acad. Sci. USA 100, 11 309-11 314. (doi:10.1073/pnas.1834451100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11309-11314
    • Paas, Y.1    Cartaud, J.2    Recouvreur, M.3    Grailhe, R.4    Dufresne, V.5    Pebay-Peyroula, E.6    Landau, E.M.7    Changeux, J.P.8
  • 15
    • 6344238642 scopus 로고    scopus 로고
    • Crystallization of transmembrane proteins in cubo: Mechanisms of crystal growth and defect formation
    • Qutub Y, Reviakine I, Maxwell C, Navarro J, Landau EM, Vekilov PG. 2004 Crystallization of transmembrane proteins in cubo: mechanisms of crystal growth and defect formation. J. Mol. Biol. 343, 1243-1254. (doi:10.1016/j.jmb.2004.09.022)
    • (2004) J. Mol. Biol. , vol.343 , pp. 1243-1254
    • Qutub, Y.1    Reviakine, I.2    Maxwell, C.3    Navarro, J.4    Landau, E.M.5    Vekilov, P.G.6
  • 16
    • 0037304543 scopus 로고    scopus 로고
    • Protein interactions and membrane geometry
    • Grabe M, Neu J, Oster G, Nollert P. 2003 Protein interactions and membrane geometry. Biophys. J. 84, 854-868. (doi:10.1016/S0006-3495(03)74904-2)
    • (2003) Biophys J. , vol.84 , pp. 854-868
    • Grabe, M.1    Neu, J.2    Oster, G.3    Nollert, P.4
  • 18
    • 77955619741 scopus 로고    scopus 로고
    • Crystallizing transmembrane peptides in lipidic mesophases
    • Hofer N, Aragao D, Caffrey M. 2010 Crystallizing transmembrane peptides in lipidic mesophases. Biophys. J. 99, L23-L25. (doi:10.1016/j.bpj.2010.05.011)
    • (2010) Biophys J. , vol.99 , pp. L23-L25
    • Hofer, N.1    Aragao, D.2    Caffrey, M.3
  • 19
    • 84929962768 scopus 로고    scopus 로고
    • Transmembrane complexes of DAP12 crystallized in lipid membranes provide insights into control of oligomerization in immunoreceptor assembly
    • Knoblich K et al. 2015 Transmembrane complexes of DAP12 crystallized in lipid membranes provide insights into control of oligomerization in immunoreceptor assembly. Cell Rep. 11, 1184-1192. (doi:10.1016/j.celrep.2015.04.045)
    • (2015) Cell Rep. , vol.11 , pp. 1184-1192
    • Knoblich, K.1
  • 20
    • 26044470166 scopus 로고    scopus 로고
    • KARAP/DAP12/TYROBP: Three names and a multiplicity of biological functions (35, pg 1670, 2005)
    • Tomasello E, Vivier E. 2005 KARAP/DAP12/TYROBP: three names and a multiplicity of biological functions (vol 35, pg 1670, 2005). Eur. J. Immunol. 35, 2776. (doi:10.1002/eji. 255590587)
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2776
    • Tomasello, E.1    Vivier, E.2
  • 21
    • 77958153191 scopus 로고    scopus 로고
    • The structural basis for intramembrane assembly of an activating immunoreceptor complex
    • Call ME, Wucherpfennig KW, Chou JJ. 2010 The structural basis for intramembrane assembly of an activating immunoreceptor complex. Nat. Immunol. 11, 1023-1029. (doi:10.1038/Ni. 1943)
    • (2010) Nat. Immunol. , vol.11 , pp. 1023-1029
    • Call, M.E.1    Wucherpfennig, K.W.2    Chou, J.J.3
  • 22
    • 0033063287 scopus 로고    scopus 로고
    • DAP12: A key accessory protein for relaying signals by natural killer cell receptors
    • Campbell KS, Colonna M. 1999 DAP12: a key accessory protein for relaying signals by natural killer cell receptors. Int. J. Biochem. Cell Biol. 31, 631-636. (doi:10.1016/S1357-2725(99)00022-9)
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 631-636
    • Campbell, K.S.1    Colonna, M.2
  • 23
    • 79951665122 scopus 로고    scopus 로고
    • Self-assembled multicompartment liquid crystalline lipid carriers for protein, peptide, and nucleic acid drug delivery
    • Angelova A, Angelov B, Mutafchieva R, Lesieur S, Couvreur P. 2011 Self-assembled multicompartment liquid crystalline lipid carriers for protein, peptide, and nucleic acid drug delivery. Acc. Chem. Res. 44, 147-156. (doi:10.1021/Ar100120v)
    • (2011) Acc. Chem. Res. , vol.44 , pp. 147-156
    • Angelova, A.1    Angelov, B.2    Mutafchieva, R.3    Lesieur, S.4    Couvreur, P.5
  • 24
    • 66049128793 scopus 로고    scopus 로고
    • Crystallizing membrane proteins for structure determination: Use of lipidic mesophases
    • Caffrey M. 2009 Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev. Biophys. 38, 29-51. (doi:10.1146/annurev.biophys.050708.133655)
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 29-51
    • Caffrey, M.1
  • 25
    • 33646478538 scopus 로고    scopus 로고
    • Incorporation of alpha-chymotrypsin into the 3D channels of bicontinuous cubic lipid mesophases
    • Kraineva J, Nicolini C, Thiyagarajan P, Kondrashkina E, Winter R. 2006 Incorporation of alpha-chymotrypsin into the 3D channels of bicontinuous cubic lipid mesophases. Biochim. Biophys. Acta. 1764, 424-433. (doi:10.1016/j.bbapap.2005.11.004)
    • (2006) Biochim. Biophys. Acta. , vol.1764 , pp. 424-433
    • Kraineva, J.1    Nicolini, C.2    Thiyagarajan, P.3    Kondrashkina, E.4    Winter, R.5
  • 26
    • 84874845048 scopus 로고    scopus 로고
    • Nanostructured bicontinuous cubic lipid self-assembly materials as matrices for protein encapsulation
    • Conn CE, Drummond CJ. 2013 Nanostructured bicontinuous cubic lipid self-assembly materials as matrices for protein encapsulation. Soft Matter 9, 3449-3464. (doi:10.1039/ C3sm27743g)
    • (2013) Soft Matter , vol.9 , pp. 3449-3464
    • Conn, C.E.1    Drummond, C.J.2
  • 27
    • 0014401350 scopus 로고
    • Structure of cubic phases of lipidwater systems
    • Luzzati V, Tardieu A, Gulikkrz T, Rivas E, Reisshus F. 1968 Structure of cubic phases of lipidwater systems. Nature 220, 485-488. (doi:10.1038/220485a0)
    • (1968) Nature , vol.220 , pp. 485-488
    • Luzzati, V.1    Tardieu, A.2    Gulikkrz, T.3    Rivas, E.4    Reisshus, F.5
  • 28
    • 84855930725 scopus 로고    scopus 로고
    • Lyotropic liquid crystal engineering-ordered nanostructured small molecule amphiphile self-assembly materials by design
    • Fong C, Le T, Drummond CJ. 2012 Lyotropic liquid crystal engineering-ordered nanostructured small molecule amphiphile self-assembly materials by design. Chem. Soc. Rev. 41, 1297-1322. (doi:10.1039/C1cs15148g)
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 1297-1322
    • Fong, C.1    Le, T.2    Drummond, C.J.3
  • 29
    • 84946950014 scopus 로고    scopus 로고
    • Deconvoluting the effect of the hydrophobic and hydrophilic domains of an amphiphilic integral membrane protein in lipid bicontinuous cubic mesophases
    • van 't Hag L, Shen HH, Lu J, Hawley AM, Gras SL, Drummond CJ, Conn CE. 2015 Deconvoluting the effect of the hydrophobic and hydrophilic domains of an amphiphilic integral membrane protein in lipid bicontinuous cubic mesophases. Langmuir. 31, 12 025-12 034. (doi:10.1021/acs.langmuir.5b03256)
    • (2015) Langmuir , vol.31 , pp. 12025-12034
    • Van 'T Hag, L.1    Shen, H.H.2    Lu, J.3    Hawley, A.M.4    Gras, S.L.5    Drummond, C.J.6    Conn, C.E.7
  • 32
    • 0030148764 scopus 로고    scopus 로고
    • The temperature-composition phase diagram and mesophase structure characterization of the monoolein/water system
    • Briggs J, Chung H, Caffrey M. 1996 The temperature-composition phase diagram and mesophase structure characterization of the monoolein/water system. J. Phys. II 6, 723-751. (doi:10.1051/jp2:1996208)
    • (1996) J. Phys. II , vol.6 , pp. 723-751
    • Briggs, J.1    Chung, H.2    Caffrey, M.3
  • 33
    • 0033992338 scopus 로고    scopus 로고
    • The phase diagram of the monoolein/water system: Metastability and equilibrium aspects
    • Qiu H, Caffrey M. 2000 The phase diagram of the monoolein/water system: metastability and equilibrium aspects. Biomaterials 21, 223-234. (doi:10.1016/S0142-9612(99)00126-X)
    • (2000) Biomaterials , vol.21 , pp. 223-234
    • Qiu, H.1    Caffrey, M.2
  • 34
    • 84923141629 scopus 로고    scopus 로고
    • Methodological advances: The unsung heroes of the GPCR structural revolution
    • Ghosh E, Kumari P, Jaiman D, Shukla AK. 2015 Methodological advances: the unsung heroes of the GPCR structural revolution. Nat. Rev. Mol. Cell Biol. 16, 69-81. (doi:10.1038/Nrm3933)
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 69-81
    • Ghosh, E.1    Kumari, P.2    Jaiman, D.3    Shukla, A.K.4
  • 35
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey M. 2003 Membrane protein crystallization. J. Struct. Biol. 142, 108-132. (doi:10.1016/ S1047-8477(03)00043-1)
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 36
    • 0033930876 scopus 로고    scopus 로고
    • A lipid's eye view of membrane protein crystallization in mesophases
    • Caffrey M. 2000 A lipid's eye view of membrane protein crystallization in mesophases. Curr. Opin. Struct. Biol. 10, 486-497. (doi:10.1016/S0959-440x(00)00119-6)
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 486-497
    • Caffrey, M.1
  • 37
    • 84882974287 scopus 로고    scopus 로고
    • Production of disulfide-stabilized transmembrane peptide complexes for structural studies
    • Sharma P, Kaywan-Lutfi M, Krshnan L, Byrne EF, Call MJ, Call ME. 2013 Production of disulfide-stabilized transmembrane peptide complexes for structural studies. J. Vis. Exp. 73, e50141. (doi:10.3791/50141)
    • (2013) J. Vis. Exp. , vol.73 , pp. e50141
    • Sharma, P.1    Kaywan-Lutfi, M.2    Krshnan, L.3    Byrne, E.F.4    Call, M.J.5    Call, M.E.6
  • 38
    • 84891692783 scopus 로고    scopus 로고
    • Using time courses to enrich the information obtained from images of crystallization trials
    • Mele K, Lekamge BMT, Fazio VJ, Newman J. 2014 Using time courses to enrich the information obtained from images of crystallization trials. Cryst. Growth Des. 14, 261-269. (doi:10.1021/Cg4014569)
    • (2014) Cryst. Growth Des. , vol.14 , pp. 261-269
    • Mele, K.1    Lekamge, B.M.T.2    Fazio, V.J.3    Newman, J.4
  • 40
    • 84897531201 scopus 로고    scopus 로고
    • In meso crystallization: Compatibility of different lipid bicontinuous cubic mesophases with the cubic crystallization screen in aqueous solution
    • van 't Hag L, Darmanin C, Le TC, Mudie S, Conn CE, Drummond CJ. 2014 In meso crystallization: compatibility of different lipid bicontinuous cubic mesophases with the cubic crystallization screen in aqueous solution. Cryst. Growth Des. 14, 1771-1781. (doi:10.1021/ Cg4018954)
    • (2014) Cryst. Growth Des. , vol.14 , pp. 1771-1781
    • Van 'T Hag, L.1    Darmanin, C.2    Le, T.C.3    Mudie, S.4    Conn, C.E.5    Drummond, C.J.6
  • 43
    • 0036929858 scopus 로고    scopus 로고
    • Membrane protein crystallization in meso: Lipid type-tailoring of the cubic phase
    • Cherezov V, Clogston J, Misquitta Y, Abdel-Gawad W, Caffrey M. 2002 Membrane protein crystallization in meso: lipid type-tailoring of the cubic phase. Biophys. J. 83, 3393-3407. (doi:10.1016/S0006-3495(02)75339-3)
    • (2002) Biophys J. , vol.83 , pp. 3393-3407
    • Cherezov, V.1    Clogston, J.2    Misquitta, Y.3    Abdel-Gawad, W.4    Caffrey, M.5
  • 44
    • 45549093635 scopus 로고    scopus 로고
    • Fractal aggregates in protein crystal nucleation
    • Chen B, Nellas RB, Keasler SJ. 2008 Fractal aggregates in protein crystal nucleation. J. Phys. Chem. B 112, 4725-4730. (doi:10.1021/Jp8002728)
    • (2008) J. Phys. Chem. B , vol.112 , pp. 4725-4730
    • Chen, B.1    Nellas, R.B.2    Keasler, S.J.3
  • 45
    • 84856733257 scopus 로고    scopus 로고
    • High-throughput analysis of the structuralevolution of the monoolein cubic phasein situ under crystallogenesis conditions
    • Conn CE, Darmanin C, Mulet X, Le Cann S, Kirby N, Drummond CJ. 2012 High-throughput analysis of the structuralevolution of the monoolein cubic phasein situ under crystallogenesis conditions. Soft Matter 8, 2310-2321. (doi:10.1039/C2sm07232g)
    • (2012) Soft Matter , vol.8 , pp. 2310-2321
    • Conn, C.E.1    Darmanin, C.2    Mulet, X.3    Le Cann, S.4    Kirby, N.5    Drummond, C.J.6
  • 46
    • 0034961077 scopus 로고    scopus 로고
    • Crystallization screens: Compatibility with the lipidic cubic phase for in meso crystallization of membrane proteins
    • Cherezov V, Fersi H, Caffrey M. 2001 Crystallization screens: compatibility with the lipidic cubic phase for in meso crystallization of membrane proteins. Biophys. J. 81, 225-242. (doi:10.1016/S0006-3495(01)75694-9)
    • (2001) Biophys J. , vol.81 , pp. 225-242
    • Cherezov, V.1    Fersi, H.2    Caffrey, M.3
  • 47
    • 84869597401 scopus 로고    scopus 로고
    • Effect of lipid architecture on cubic phase susceptibility to crystallisation screens
    • Conn CE, Darmanin C, Mulet X, Hawley A, Drummond CJ. 2012 Effect of lipid architecture on cubic phase susceptibility to crystallisation screens. Soft Matter 8, 6884-6896. (doi:10.1039/c2sm25705j)
    • (2012) Soft Matter , vol.8 , pp. 6884-6896
    • Conn, C.E.1    Darmanin, C.2    Mulet, X.3    Hawley, A.4    Drummond, C.J.5
  • 48
    • 70349548901 scopus 로고    scopus 로고
    • Observing self-assembled lipid nanoparticles building order and complexity through low-energy transformation processes
    • Mulet X, Gong X, Waddington LJ, Drummond CJ. 2009 Observing self-assembled lipid nanoparticles building order and complexity through low-energy transformation processes. ACS Nano. 3, 2789-2797. (doi:10.1021/nn900671u)
    • (2009) ACS Nano , vol.3 , pp. 2789-2797
    • Mulet, X.1    Gong, X.2    Waddington, L.J.3    Drummond, C.J.4
  • 49
    • 84871806275 scopus 로고    scopus 로고
    • Modulating the crystal size and morphology of in mesocrystallized lysozyme by precisely controlling the water channel size of the hosting mesophase
    • Zabara A, Mezzenga R. 2013 Modulating the crystal size and morphology of in mesocrystallized lysozyme by precisely controlling the water channel size of the hosting mesophase. Soft Matter 9, 1010-1014. (doi:10.1039/C2sm26988k)
    • (2013) Soft Matter , vol.9 , pp. 1010-1014
    • Zabara, A.1    Mezzenga, R.2
  • 50
    • 5544258281 scopus 로고    scopus 로고
    • Crystallization of a polar protein and small molecules from the aqueous compartment of lipidic cubic phases
    • Landau EM, Rummel G, CowanJacob SW, Rosenbusch JP. 1997 Crystallization of a polar protein and small molecules from the aqueous compartment of lipidic cubic phases. J. Phys. Chem. B 101, 1935-1937. (doi:10.1021/Jp963347q)
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1935-1937
    • Landau, E.M.1    Rummel, G.2    CowanJacob, S.W.3    Rosenbusch, J.P.4


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