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Volumn 109, Issue 41, 2012, Pages

Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis

Author keywords

Extended X ray absorption fine structure; Isomerohydrolase; Metalloprotein; Monotopic membrane protein

Indexed keywords

IRON; ISOMERASE; METALLOPROTEIN; PHOSPHOLIPID; RETINOID; RPE65 ISOMERASE; UNCLASSIFIED DRUG;

EID: 84867345070     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212025109     Document Type: Article
Times cited : (53)

References (66)
  • 1
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski K (2006) G protein-coupled receptor rhodopsin. Annu Rev Biochem 75:743-767.
    • (2006) Annu Rev Biochem , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 2
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • Choe HW, et al. (2011) Crystal structure of metarhodopsin II. Nature 471:651-655.
    • (2011) Nature , vol.471 , pp. 651-655
    • Choe, H.W.1
  • 4
    • 77953685640 scopus 로고    scopus 로고
    • The biochemical and structural basis for trans-to-cis isomerization of retinoids in the chemistry of vision
    • von Lintig J, Kiser PD, Golczak M, Palczewski K (2010) The biochemical and structural basis for trans-to-cis isomerization of retinoids in the chemistry of vision. Trends Biochem Sci 35:400-410.
    • (2010) Trends Biochem Sci , vol.35 , pp. 400-410
    • Von Lintig, J.1    Kiser, P.D.2    Golczak, M.3    Palczewski, K.4
  • 5
    • 0014428724 scopus 로고
    • The molecular basis of visual excitation
    • Wald G (1968) The molecular basis of visual excitation. Nature 219:800-807.
    • (1968) Nature , vol.219 , pp. 800-807
    • Wald, G.1
  • 6
    • 0031255068 scopus 로고    scopus 로고
    • Mutations in RPE65 cause autosomal recessive childhood-onset severe retinal dystrophy
    • Gu SM, et al. (1997) Mutations in RPE65 cause autosomal recessive childhood-onset severe retinal dystrophy. Nat Genet 17:194-197.
    • (1997) Nat Genet , vol.17 , pp. 194-197
    • Gu, S.M.1
  • 7
    • 0031252434 scopus 로고    scopus 로고
    • Mutations in RPE65 cause Leber's congenital amaurosis
    • Marlhens F, et al. (1997) Mutations in RPE65 cause Leber's congenital amaurosis. Nat Genet 17:139-141.
    • (1997) Nat Genet , vol.17 , pp. 139-141
    • Marlhens, F.1
  • 9
    • 0027242119 scopus 로고
    • Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro
    • Hamel CP, et al. (1993) Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro. J Biol Chem 268:15751-15757. (Pubitemid 23222076)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.21 , pp. 15751-15757
    • Hamel, C.P.1    Tsilou, E.2    Pfeffer, B.A.3    Hooks, J.J.4    Detrick, B.5    Redmond, T.M.6
  • 10
    • 65549131951 scopus 로고    scopus 로고
    • Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane
    • Nikolaeva O, Takahashi Y, Moiseyev G, Ma JX (2009) Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane. FEBS J 276:3020-3030.
    • (2009) FEBS J , vol.276 , pp. 3020-3030
    • Nikolaeva, O.1    Takahashi, Y.2    Moiseyev, G.3    Ma, J.X.4
  • 11
    • 77951229802 scopus 로고    scopus 로고
    • Importance of membrane structural integrity for RPE65 retinoid isomerization activity
    • Golczak M, Kiser PD, Lodowski DT, Maeda A, Palczewski K (2010) Importance of membrane structural integrity for RPE65 retinoid isomerization activity. J Biol Chem 285:9667-9682.
    • (2010) J Biol Chem , vol.285 , pp. 9667-9682
    • Golczak, M.1    Kiser, P.D.2    Lodowski, D.T.3    Maeda, A.4    Palczewski, K.5
  • 12
    • 79957740398 scopus 로고    scopus 로고
    • Binding to lipid membrane induces conformational changes in RPE65: Implications for its isomerohydrolase activity
    • Nikolaeva O, Moiseyev G, Rodgers KK, Ma JX (2011) Binding to lipid membrane induces conformational changes in RPE65: Implications for its isomerohydrolase activity. Biochem J 436:591-597.
    • (2011) Biochem J , vol.436 , pp. 591-597
    • Nikolaeva, O.1    Moiseyev, G.2    Rodgers, K.K.3    Ma, J.X.4
  • 15
    • 0033605656 scopus 로고    scopus 로고
    • Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein
    • DOI 10.1074/jbc.274.13.8577
    • Stecher H, Gelb MH, Saari JC, Palczewski K (1999) Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. J Biol Chem 274:8577-8585. (Pubitemid 29164649)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8577-8585
    • Stecher, H.1    Gelb, M.H.2    Saari, J.C.3    Palczewski, K.4
  • 16
    • 76249086955 scopus 로고    scopus 로고
    • RPE65, visual cycle retinol isomerase, is not inherently 11-cis-specific: Support for a carbocation mechanism of retinol isomerization
    • Redmond TM, Poliakov E, Kuo S, Chander P, Gentleman S (2010) RPE65, visual cycle retinol isomerase, is not inherently 11-cis-specific: Support for a carbocation mechanism of retinol isomerization. J Biol Chem 285:1919-1927.
    • (2010) J Biol Chem , vol.285 , pp. 1919-1927
    • Redmond, T.M.1    Poliakov, E.2    Kuo, S.3    Chander, P.4    Gentleman, S.5
  • 17
    • 0034687090 scopus 로고    scopus 로고
    • Isomerization of all-trans-retinol to cis-retinols in bovine retinal pigment epithelial cells: Dependence on the specificity of retinoid-binding proteins
    • McBee JK, et al. (2000) Isomerization of all-trans-retinol to cis-retinols in bovine retinal pigment epithelial cells: Dependence on the specificity of retinoid-binding proteins. Biochemistry 39:11370-11380.
    • (2000) Biochemistry , vol.39 , pp. 11370-11380
    • McBee, J.K.1
  • 18
    • 33747623998 scopus 로고    scopus 로고
    • Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
    • DOI 10.1038/sj.emboj.7601237, PII 7601237
    • Yildiz O, Vinothkumar KR, Goswami P, Kühlbrandt W (2006) Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J 25:3702-3713. (Pubitemid 44264880)
    • (2006) EMBO Journal , vol.25 , Issue.15 , pp. 3702-3713
    • Yildiz, O.1    Vinothkumar, K.R.2    Goswami, P.3    Kuhlbrandt, W.4
  • 19
    • 0034084540 scopus 로고    scopus 로고
    • Objective comparison of protein structures: Error-scaled difference distance matrices
    • Schneider TR (2000) Objective comparison of protein structures: Error-scaled difference distance matrices. Acta Crystallogr D Biol Crystallogr 56:714-721.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 714-721
    • Schneider, T.R.1
  • 21
    • 0001352661 scopus 로고
    • X-ray-absorption pre-edge studies of high-spin iron(II) complexes
    • Randall CR, et al. (1995) X-ray-absorption pre-edge studies of high-spin iron(II) complexes. Inorg Chem 34:1036-1039.
    • (1995) Inorg Chem , vol.34 , pp. 1036-1039
    • Randall, C.R.1
  • 22
    • 36549086621 scopus 로고    scopus 로고
    • Structural "snapshots" along reaction pathways of non-heme iron enzymes
    • DOI 10.1002/anie.200703057
    • Emerson JP, Farquhar ER, Que L, Jr. (2007) Structural "snapshots" along reaction pathways of non-heme iron enzymes. Angew Chem Int Ed Engl 46:8553-8556. (Pubitemid 350189065)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.45 , pp. 8553-8556
    • Emerson, J.P.1    Farquhar, E.R.2    Que Jr., L.3
  • 24
    • 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.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 559-566
    • Cherezov, V.1
  • 25
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • DOI 10.1006/jmbi.2001.5295
    • Faham S, Bowie JU (2002) Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J Mol Biol 316:1-6. (Pubitemid 34729261)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.1 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 26
    • 67650282016 scopus 로고    scopus 로고
    • Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment
    • Raunser S, Walz T (2009) Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment. Annu Rev Biophys 38:89-105.
    • (2009) Annu Rev Biophys , vol.38 , pp. 89-105
    • Raunser, S.1    Walz, T.2
  • 28
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution
    • DOI 10.1038/sj.emboj.7600585
    • Standfuss J, Terwisscha van Scheltinga AC, Lamborghini M, Kühlbrandt W (2005) Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution. EMBO J 24:919-928. (Pubitemid 40470141)
    • (2005) EMBO Journal , vol.24 , Issue.5 , pp. 919-928
    • Standfuss, J.1    Van Scheltinga, A.C.T.2    Lamborghini, M.3    Kuhlbrandt, W.4
  • 30
    • 79958013764 scopus 로고    scopus 로고
    • HiLiDe-systematic approach to membrane protein crystallization in lipid and detergent
    • Gourdon P, et al. (2011) HiLiDe-systematic approach to membrane protein crystallization in lipid and detergent. Cryst Growth Des 11:2098-2106.
    • (2011) Cryst Growth des , vol.11 , pp. 2098-2106
    • Gourdon, P.1
  • 31
    • 2942564630 scopus 로고    scopus 로고
    • Structural commonalities among integral membrane enzymes
    • DOI 10.1016/j.febslet.2004.04.084, PII S0014579304005733
    • Bracey MH, Cravatt BF, Stevens RC (2004) Structural commonalities among integral membrane enzymes. FEBS Lett 567:159-165. (Pubitemid 38748385)
    • (2004) FEBS Letters , vol.567 , Issue.2-3 , pp. 159-165
    • Bracey, M.H.1    Cravatt, B.F.2    Stevens, R.C.3
  • 32
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling
    • DOI 10.1126/science.1076535
    • Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (2002) Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling. Science 298:1793-1796. (Pubitemid 35404124)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 33
    • 16444383613 scopus 로고    scopus 로고
    • The structure of a retinal-forming carotenoid oxygenase
    • DOI 10.1126/science.1108965
    • Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE (2005) The structure of a retinal-forming carotenoid oxygenase. Science 308:267-269. (Pubitemid 40558865)
    • (2005) Science , vol.308 , Issue.5719 , pp. 267-269
    • Kloer, D.P.1    Ruch, S.2    Al-Babili, S.3    Beyer, P.4    Schulz, G.E.5
  • 34
    • 33846018938 scopus 로고    scopus 로고
    • Identification of carotenoid cleavage dioxygenases from Nostoc sp. PCC 7120 with different cleavage activities
    • DOI 10.1074/jbc.M606299200
    • Marasco EK, Vay K, Schmidt-Dannert C (2006) Identification of carotenoid cleavage dioxygenases from Nostoc sp. PCC 7120 with different cleavage activities. J Biol Chem 281:31583-31593. (Pubitemid 46041424)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31583-31593
    • Marasco, E.K.1    Vay, K.2    Schmidt-Dannert, C.3
  • 35
    • 14544289081 scopus 로고    scopus 로고
    • Retinal biosynthesis in Eubacteria: In vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803
    • DOI 10.1111/j.1365-2958.2004.04460.x
    • Ruch S, Beyer P, Ernst H, Al-Babili S (2005) Retinal biosynthesis in Eubacteria: In vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803. Mol Microbiol 55:1015-1024. (Pubitemid 40299173)
    • (2005) Molecular Microbiology , vol.55 , Issue.4 , pp. 1015-1024
    • Ruch, S.1    Beyer, P.2    Ernst, H.3    Al-Babili, S.4
  • 36
    • 33748757737 scopus 로고    scopus 로고
    • Retinal is formed from apo-carotenoids in Nostoc sp. PCC7120: In vitro characterization of an apo-carotenoid oxygenase
    • DOI 10.1042/BJ20060592
    • Scherzinger D, Ruch S, Kloer DP, Wilde A, Al-Babili S (2006) Retinal is formed from apo-carotenoids in Nostoc sp. PCC7120: In vitro characterization of an apo-carotenoid oxygenase. Biochem J 398:361-369. (Pubitemid 44453380)
    • (2006) Biochemical Journal , vol.398 , Issue.3 , pp. 361-369
    • Scherzinger, D.1    Ruch, S.2    Kloer, D.P.3    Wilde, A.4    Al-Babili, S.5
  • 37
    • 0024311947 scopus 로고
    • Solubilization and partial purification of retinyl ester synthetase and retinoid isomerase from bovine ocular pigment epithelium
    • Barry RJ, Cañada FJ, Rando RR (1989) Solubilization and partial purification of retinyl ester synthetase and retinoid isomerase from bovine ocular pigment epithelium. J Biol Chem 264:9231-9238. (Pubitemid 19157558)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.16 , pp. 9231-9238
    • Barry, R.J.1    Canada, F.J.2    Rando, R.R.3
  • 38
    • 0023020106 scopus 로고
    • In vivo isomerization of all-trans- to 11-cis-retinoids in the eye occurs at the alcohol oxidation state
    • Bernstein PS, Rando RR (1986) In vivo isomerization of all-trans- to 11-cis-retinoids in the eye occurs at the alcohol oxidation state. Biochemistry 25:6473-6478. (Pubitemid 17217896)
    • (1986) Biochemistry , vol.25 , Issue.21 , pp. 6473-6478
    • Bernstein, P.S.1    Rando, R.R.2
  • 39
    • 0034623239 scopus 로고    scopus 로고
    • Stereoisomeric specificity of the retinoid cycle in the vertebrate retina
    • Jang GF, McBee JK, Alekseev AM, Haeseleer F, Palczewski K (2000) Stereoisomeric specificity of the retinoid cycle in the vertebrate retina. J Biol Chem 275:28128-28138.
    • (2000) J Biol Chem , vol.275 , pp. 28128-28138
    • Jang, G.F.1    McBee, J.K.2    Alekseev, A.M.3    Haeseleer, F.4    Palczewski, K.5
  • 40
    • 0024300825 scopus 로고
    • Stereochemical inversion at C-15 accompanies the enzymatic isomerization of all-trans- To 11-cis-retinoids
    • Law WC, Rando RR (1988) Stereochemical inversion at C-15 accompanies the enzymatic isomerization of all-trans- to 11-cis-retinoids. Biochemistry 27:4147-4152.
    • (1988) Biochemistry , vol.27 , pp. 4147-4152
    • Law, W.C.1    Rando, R.R.2
  • 42
    • 77954620409 scopus 로고    scopus 로고
    • Membrane-binding and enzymatic properties of RPE65
    • Kiser PD, Palczewski K (2010) Membrane-binding and enzymatic properties of RPE65. Prog Retin Eye Res 29:428-442.
    • (2010) Prog Retin Eye Res , vol.29 , pp. 428-442
    • Kiser, P.D.1    Palczewski, K.2
  • 43
    • 80052757041 scopus 로고    scopus 로고
    • Alpha-phenyl-N-tert-butylnitrone (PBN) prevents light-induced degeneration of the retina by inhibiting RPE65 protein isomerohydrolase activity
    • Mandal MN, et al. (2011) Alpha-phenyl-N-tert-butylnitrone (PBN) prevents light-induced degeneration of the retina by inhibiting RPE65 protein isomerohydrolase activity. J Biol Chem 286:32491-32501.
    • (2011) J Biol Chem , vol.286 , pp. 32491-32501
    • Mandal, M.N.1
  • 44
    • 84865764391 scopus 로고    scopus 로고
    • Aromatic residues in the substrate cleft of RPE65 govern retinol isomerization and modulate its progression
    • Chander P, Gentleman S, Poliakov E, Redmond TM (2012) Aromatic residues in the substrate cleft of RPE65 govern retinol isomerization and modulate its progression. J Biol Chem 287:30552-30559.
    • (2012) J Biol Chem , vol.287 , pp. 30552-30559
    • Chander, P.1    Gentleman, S.2    Poliakov, E.3    Redmond, T.M.4
  • 45
    • 0033605220 scopus 로고    scopus 로고
    • Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid
    • DOI 10.1006/jmbi.1998.2532
    • Lancaster CR, Michel H (1999) Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid. J Mol Biol 286:883-898. (Pubitemid 29106224)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.3 , pp. 883-898
    • Lancaster, C.R.D.1    Michel, H.2
  • 46
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the Photosynthetic Oxygen-Evolving Center
    • DOI 10.1126/science.1093087
    • Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303:1831-1838. (Pubitemid 38374869)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 47
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • Gillmor SA, Villaseñor A, Fletterick R, Sigal E, Browner MF (1997) The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat Struct Biol 4:1003-1009. (Pubitemid 27525804)
    • (1997) Nature Structural Biology , vol.4 , Issue.12 , pp. 1003-1009
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 48
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que L, Jr., Ho RY (1996) Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 96:2607-2624.
    • (1996) Chem Rev , vol.96 , pp. 2607-2624
    • Que Jr., L.1    Ho, R.Y.2
  • 49
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm RH, Kennepohl P, Solomon EI (1996) Structural and functional aspects of metal sites in biology. Chem Rev 96:2239-2314. (Pubitemid 126641104)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 50
    • 0020170339 scopus 로고
    • Evidence for a spin-coupled binuclear iron unit at the active site of the purple acid phosphatase from beef spleen
    • Davis JC, Averill BA (1982) Evidence for a spin-coupled binuclear iron unit at the active site of the purple acid phosphatase from beef spleen. Proc Natl Acad Sci USA 79:4623-4627.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4623-4627
    • Davis, J.C.1    Averill, B.A.2
  • 51
    • 0033600583 scopus 로고    scopus 로고
    • The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme
    • D'souza VM, Holz RC (1999) The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. Biochemistry 38:11079-11085.
    • (1999) Biochemistry , vol.38 , pp. 11079-11085
    • D'souza, V.M.1    Holz, R.C.2
  • 52
    • 0000296163 scopus 로고    scopus 로고
    • Peptide deformylase: A new type of mononuclear iron protein
    • Rajagopalan PTR, Yu XC, Pei DH (1997) Peptide deformylase: A new type of mononuclear iron protein. J Am Chem Soc 119:12418-12419.
    • (1997) J Am Chem Soc , vol.119 , pp. 12418-12419
    • Rajagopalan, P.T.R.1    Yu, X.C.2    Pei, D.H.3
  • 53
    • 0028835678 scopus 로고
    • Mechanism of extradiol catechol dioxygenases - Evidence for a lactone intermediate in the 2,3-dihydroxyphenylpropionate 1,2-dioxygenase reaction
    • Sanvoisin J, Langley GJ, Bugg TDH (1995) Mechanism of extradiol catechol dioxygenases - Evidence for a lactone intermediate in the 2,3- dihydroxyphenylpropionate 1,2-dioxygenase reaction. J Am Chem Soc 117:7836-7837.
    • (1995) J Am Chem Soc , vol.117 , pp. 7836-7837
    • Sanvoisin, J.1    Langley, G.J.2    Bugg, T.D.H.3
  • 54
    • 0033591960 scopus 로고    scopus 로고
    • Probing the role of the trivalent metal in phosphate ester hydrolysis: Preparation and characterization of purple acid phosphatases containing (AlZnII)-Zn-III and (InZnII)-Zn-III active sites, including the first example of an active aluminum enzyme
    • Merkx M, Averill BA (1999) Probing the role of the trivalent metal in phosphate ester hydrolysis: Preparation and characterization of purple acid phosphatases containing (AlZnII)-Zn-III and (InZnII)-Zn-III active sites, including the first example of an active aluminum enzyme. J Am Chem Soc 121:6683-6689.
    • (1999) J Am Chem Soc , vol.121 , pp. 6683-6689
    • Merkx, M.1    Averill, B.A.2
  • 56
    • 0000952473 scopus 로고
    • Treatment of negative intensity observations
    • French S, Wilson K (1978) Treatment of negative intensity observations. Acta Crystallogr A 34:517-525.
    • (1978) Acta Crystallogr A , vol.34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 57
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67:235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 60
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick GM (2010) Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr 66:479-485.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 61
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov GN, et al. (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67:355-367.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 63
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66:12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 64
    • 0542395209 scopus 로고    scopus 로고
    • Real-space multiple-scattering calculation and interpretation of x-ray-absorption near-edge structure
    • Ankudinov AL, Ravel B, Rehr JJ, Conradson SD (1998) Real-space multiple-scattering calculation and interpretation of x-ray-absorption near-edge structure. Phys Rev B 58:7565.
    • (1998) Phys Rev B , vol.58 , pp. 7565
    • Ankudinov, A.L.1    Ravel, B.2    Rehr, J.J.3    Conradson, S.D.4
  • 65
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenström P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-W549.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Holm, L.1    Rosenström, P.2
  • 66
    • 0000330205 scopus 로고    scopus 로고
    • On the use of the merging R factor as a quality indicator for X-ray data
    • Weiss MS, Hilgenfeld R (1997) On the use of the merging R factor as a quality indicator for X-ray data. J Appl Cryst 30:203-205. (Pubitemid 127477069)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.2 , pp. 203-205
    • Weiss, M.S.1    Hilgenfeld, R.2


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