메뉴 건너뛰기




Volumn 111, Issue 32, 2014, Pages 11709-11714

Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy

Author keywords

3D reconstruction; CTF determination; Frame alignment; Single particle EM; Structure refinement

Indexed keywords

BETA GALACTOSIDASE; MEMBRANE PROTEIN; MULTIPROTEIN COMPLEX; VANILLOID RECEPTOR 1;

EID: 84905974179     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1402809111     Document Type: Article
Times cited : (172)

References (48)
  • 1
    • 67649807795 scopus 로고    scopus 로고
    • Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM
    • Chen JZ, et al. (2009) Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc Natl Acad Sci USA 106(26):10644-10648
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.26 , pp. 10644-10648
    • Chen, J.Z.1
  • 2
    • 77954384340 scopus 로고    scopus 로고
    • Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus
    • Liu X, et al. (2010) Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus. Nat Struct Mol Biol 17(7):830-836
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.7 , pp. 830-836
    • Liu, X.1
  • 3
    • 84879038703 scopus 로고    scopus 로고
    • De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy
    • Mills DJ, Vitt S, Strauss M, Shima S, Vonck J (2013) De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. eLife 2:e00218
    • (2013) ELife , vol.2
    • Mills, D.J.1    Vitt, S.2    Strauss, M.3    Shima, S.4    Vonck, J.5
  • 5
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S, Henderson R (2000) Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406(6796):653-657
    • (2000) Nature , vol.406 , Issue.6796 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 6
    • 0030926720 scopus 로고    scopus 로고
    • The three-dimensional structure of aquaporin-1
    • Walz T, et al. (1997) The three-dimensional structure of aquaporin-1. Nature 387(6633):624-627
    • (1997) Nature , vol.387 , Issue.6633 , pp. 624-627
    • Walz, T.1
  • 7
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryoelectron microscopy
    • Yu X, Jin L, Zhou ZH (2008) 3.88 A structure of cytoplasmic polyhedrosis virus by cryoelectron microscopy. Nature 453(7193):415-419
    • (2008) Nature , vol.453 , Issue.7193 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zh, Z.3
  • 8
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Hui WH, Zhou ZH (2010) 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141(3):472-482
    • (2010) Cell , vol.141 , Issue.3 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zh, Z.5
  • 9
    • 41149086034 scopus 로고    scopus 로고
    • Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction
    • Zhang X, et al. (2008) Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction. Proc Natl Acad Sci USA 105(6):1867-1872
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.6 , pp. 1867-1872
    • Zhang, X.1
  • 10
    • 84898761737 scopus 로고    scopus 로고
    • Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector
    • Allegretti M, Mills DJ, McMullan G, Kühlbrandt W, Vonck J (2014) Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector. eLife 3:e01963
    • (2014) ELife , vol.3
    • Allegretti, M.1    Mills, D.J.2    McMullan, G.3    Kühlbrandt, W.4    Vonck, J.5
  • 11
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM
    • Li X, et al. (2013) Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM. Nat Methods 10(6):584-590
    • (2013) Nat Methods , vol.10 , Issue.6 , pp. 584-590
    • Li, X.1
  • 12
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao M, Cao E, Julius D, Cheng Y (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504(7478):107-112
    • (2013) Nature , vol.504 , Issue.7478 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 13
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to nearatomic resolution from thirty thousand cryo-EM particles
    • Bai XC, Fernandez IS, McMullan G, Scheres SH (2013) Ribosome structures to nearatomic resolution from thirty thousand cryo-EM particles. eLife 2:e00461
    • (2013) ELife , vol.2
    • Bai, X.C.1    Fernandez, I.S.2    Mc Mullan, G.3    Scheres, S.H.4
  • 14
    • 84887101681 scopus 로고    scopus 로고
    • Molecular architecture of a eukaryotic translational initiation complex
    • Fernández IS, et al. (2013) Molecular architecture of a eukaryotic translational initiation complex. Science 342(6160):1240585
    • (2013) Science , vol.342 , Issue.6160 , pp. 1240585
    • Fernández, I.S.1
  • 15
    • 84892797558 scopus 로고    scopus 로고
    • Architecture of the large subunit of the mammalian mitochondrial ribosome
    • Greber BJ, et al. (2014) Architecture of the large subunit of the mammalian mitochondrial ribosome. Nature 505(7484):515-519
    • (2014) Nature , vol.505 , Issue.7484 , pp. 515-519
    • Greber, B.J.1
  • 16
    • 0024007766 scopus 로고
    • Cryo-electron microscopy of vitrified specimens
    • Dubochet J, et al. (1988) Cryo-electron microscopy of vitrified specimens. Q Rev Biophys 21(2):129-228
    • (1988) Q Rev Biophys , vol.21 , Issue.2 , pp. 129-228
    • Dubochet, J.1
  • 17
    • 84870331069 scopus 로고    scopus 로고
    • LacZ beta-galactosidase: Structure and function of an enzyme of historical and molecular biological importance
    • Juers DH, Matthews BW, Huber RE (2012) LacZ beta-galactosidase: Structure and function of an enzyme of historical and molecular biological importance. Protein Sci 21(12):1792-1807
    • (2012) Protein Sci , vol.21 , Issue.12 , pp. 1792-1807
    • Juers, D.H.1    Matthews, B.W.2    Huber, R.E.3
  • 18
    • 0000755182 scopus 로고
    • Contributions of studies on the beta-galactosidase of Escherichia coli to our understanding of enzyme synthesis
    • Cohn M (1957) Contributions of studies on the beta-galactosidase of Escherichia coli to our understanding of enzyme synthesis. Bacteriol Rev 21(3):140-168
    • (1957) Bacteriol Rev , vol.21 , Issue.3 , pp. 140-168
    • Cohn, M.1
  • 19
    • 0014940536 scopus 로고
    • The amino acid sequence of beta galactosidase. I. Isolation and composition of tryptic peptides
    • Fowler AV, Zabin I (1970) The amino acid sequence of beta galactosidase. I. Isolation and composition of tryptic peptides. J Biol Chem 245(19):5032-5041
    • (1970) J Biol Chem , vol.245 , Issue.19 , pp. 5032-5041
    • Fowler, A.V.1    Zabin, I.2
  • 20
    • 0020689671 scopus 로고
    • Sequence of the lacZ gene of Escherichia coli
    • Kalnins A, Otto K, Rüther U, Müller-Hill B (1983) Sequence of the lacZ gene of Escherichia coli. EMBO J 2(4):593-597
    • (1983) EMBO J , vol.2 , Issue.4 , pp. 593-597
    • Kalnins, A.1    Otto, K.2    Rüther, U.3    Müller-Hill, B.4
  • 21
    • 0033820067 scopus 로고    scopus 로고
    • High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation
    • Juers DH, et al. (2000) High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Sci 9(9):1685-1699
    • (2000) Protein Sci , vol.9 , Issue.9 , pp. 1685-1699
    • Juers, D.H.1
  • 22
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang G, et al. (2007) EMAN2: An extensible image processing suite for electron microscopy. J Struct Biol 157(1):38-46
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1
  • 23
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • Grigorieff N (2007) FREALIGN: High-resolution refinement of single particle structures. J Struct Biol 157(1):117-125
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 117-125
    • Grigorieff, N.1
  • 24
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH (2012) RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180(3):519-530
    • (2012) J Struct Biol , vol.180 , Issue.3 , pp. 519-530
    • Scheres, S.H.1
  • 25
    • 0028178377 scopus 로고
    • Three-dimensional structure of beta-galactosidase from E. Coli
    • Jacobson RH, Zhang XJ, DuBose RF, Matthews BW (1994) Three-dimensional structure of beta-galactosidase from E. coli. Nature 369(6483):761-766
    • (1994) Nature , vol.369 , Issue.6483 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    Dubose, R.F.3    Matthews, B.W.4
  • 26
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka K, et al. (1999) The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: Implication of the charge distribution. J Mol Biol 286(3): 861-882
    • (1999) J Mol Biol , vol.286 , Issue.3 , pp. 861-882
    • Mitsuoka, K.1
  • 27
    • 0015106320 scopus 로고
    • Limitations to significant information in biological electron microscopy as a result of radiation damage
    • Glaeser RM (1971) Limitations to significant information in biological electron microscopy as a result of radiation damage. J Ultrastruct Res 36(3):466-482
    • (1971) J Ultrastruct Res , vol.36 , Issue.3 , pp. 466-482
    • Glaeser, R.M.1
  • 28
    • 0017873876 scopus 로고
    • Radiation damage relative to transmission electron microscopy of biological specimens at low temperature: A review
    • Glaeser RM, Taylor KA (1978) Radiation damage relative to transmission electron microscopy of biological specimens at low temperature: A review. J Microsc 112(1): 127-138
    • (1978) J Microsc , vol.112 , Issue.1 , pp. 127-138
    • Glaeser, R.M.1    Taylor, K.A.2
  • 29
    • 0026523919 scopus 로고
    • Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice
    • Henderson R (1992) Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice. Ultramicroscopy 46(1-4):1-18
    • (1992) Ultramicroscopy , vol.46 , Issue.1-4 , pp. 1-18
    • Henderson, R.1
  • 30
    • 0026587123 scopus 로고
    • Effects of radiation damage with 400-kV electrons on frozen, hydrated actin bundles
    • Schmid MF, Jakana J, Matsudaira P, Chiu W (1992) Effects of radiation damage with 400-kV electrons on frozen, hydrated actin bundles. J Struct Biol 108(1):62-68
    • (1992) J Struct Biol , vol.108 , Issue.1 , pp. 62-68
    • Schmid, M.F.1    Jakana, J.2    Matsudaira, P.3    Chiu, W.4
  • 31
    • 77950813607 scopus 로고    scopus 로고
    • Radiation damage in macromolecular crystallography: What is it and why should we care
    • Garman EF (2010) Radiation damage in macromolecular crystallography: What is it and why should we care? Acta Crystallogr D Biol Crystallogr 66(Pt 4):339-351
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 4 , pp. 339-351
    • Garman, E.F.1
  • 32
    • 33645498518 scopus 로고    scopus 로고
    • Experimental determination of the radiation dose limit for cryocooled protein crystals
    • Owen RL, Rudiño-Piñera E, Garman EF (2006) Experimental determination of the radiation dose limit for cryocooled protein crystals. Proc Natl Acad Sci USA 103(13): 4912-4917
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.13 , pp. 4912-4917
    • Owen, R.L.1    Rudiño-Piñera, E.2    Garman, E.F.3
  • 33
    • 12944269052 scopus 로고    scopus 로고
    • Specific chemical and structural damage to proteins produced by synchrotron radiation
    • WeikM, et al. (2000) Specific chemical and structural damage to proteins produced by synchrotron radiation. Proc Natl Acad Sci USA 97(2):623-628
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.2 , pp. 623-628
    • Weik, M.1
  • 34
    • 84859405812 scopus 로고    scopus 로고
    • Fabs enable single particle cryoEM studies of small proteins
    • Wu S, et al. (2012) Fabs enable single particle cryoEM studies of small proteins. Structure 20(4):582-592
    • (2012) Structure , vol.20 , Issue.4 , pp. 582-592
    • Wu, S.1
  • 35
    • 84890196626 scopus 로고    scopus 로고
    • Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy
    • Bartesaghi A, Merk A, Borgnia MJ, Milne JL, Subramaniam S (2013) Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat Struct Mol Biol 20(12):1352-1357
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.12 , pp. 1352-1357
    • Bartesaghi, A.1    Merk, A.2    Borgnia, M.J.3    Milne, J.L.4    Subramaniam, S.5
  • 36
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • Scheres SH, et al. (2007) Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nat Methods 4(1):27-29
    • (2007) Nat Methods , vol.4 , Issue.1 , pp. 27-29
    • Scheres, S.H.1
  • 37
    • 57049145347 scopus 로고    scopus 로고
    • Heterogeneity of large macromolecular complexes revealed by 3D cryo-EM variance analysis
    • Zhang W, Kimmel M, Spahn CM, Penczek PA (2008) Heterogeneity of large macromolecular complexes revealed by 3D cryo-EM variance analysis. Structure 16(12): 1770-1776
    • (2008) Structure , vol.16 , Issue.12 , pp. 1770-1776
    • Zhang, W.1    Kimmel, M.2    Spahn, C.M.3    Penczek, P.A.4
  • 38
    • 33845296470 scopus 로고    scopus 로고
    • SPARX, a new environment for Cryo-EM image processing
    • Hohn M, et al. (2007) SPARX, a new environment for Cryo-EM image processing. J Struct Biol 157(1):47-55
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 47-55
    • Hohn, M.1
  • 39
    • 84879841018 scopus 로고    scopus 로고
    • Structure and conformational variability of the mycobacterium tuberculosis fatty acid synthase multienzyme complex
    • Ciccarelli L, et al. (2013) Structure and conformational variability of the mycobacterium tuberculosis fatty acid synthase multienzyme complex. Structure 21(7):1251-1257
    • (2013) Structure , vol.21 , Issue.7 , pp. 1251-1257
    • Ciccarelli, L.1
  • 40
    • 84862783740 scopus 로고    scopus 로고
    • Beam-induced motion of vitrified specimen on holey carbon film
    • Brilot AF, et al. (2012) Beam-induced motion of vitrified specimen on holey carbon film. J Struct Biol 177(3):630-637
    • (2012) J Struct Biol , vol.177 , Issue.3 , pp. 630-637
    • Brilot, A.F.1
  • 41
    • 84868573207 scopus 로고    scopus 로고
    • Movies of ice-embedded particles enhance resolution in electron cryo-microscopy
    • Campbell MG, et al. (2012) Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. Structure 20(11):1823-1828
    • (2012) Structure , vol.20 , Issue.11 , pp. 1823-1828
    • Campbell, M.G.1
  • 42
    • 76749094569 scopus 로고    scopus 로고
    • The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals
    • Baker LA, Smith EA, Bueler SA, Rubinstein JL (2010) The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals. J Struct Biol 169(3):431-437
    • (2010) J Struct Biol , vol.169 , Issue.3 , pp. 431-437
    • Baker, L.A.1    Smith, E.A.2    Bueler, S.A.3    Rubinstein, J.L.4
  • 43
    • 84905217139 scopus 로고    scopus 로고
    • Single-particle cryo-electron microscopy (Cryo-EM): Progress, challenges and perspectives for further improvement
    • Agard DA, Cheng Y, Glaeser RM, Subramaniam S (2014) Single-particle cryo-electron microscopy (Cryo-EM): Progress, challenges and perspectives for further improvement. Adv Imaging Electron Phys 185:113-137
    • (2014) Adv Imaging Electron Phys , vol.185 , pp. 113-137
    • Agard, D.A.1    Cheng, Y.2    Glaeser, R.M.3    Subramaniam, S.4
  • 44
    • 0029003107 scopus 로고
    • Thepotential andlimitations of neutrons,electronsandX-rays for atomic resolution microscopy of unstained biological molecules
    • HendersonR(1995)Thepotential andlimitations of neutrons,electronsandX- rays for atomic resolution microscopy of unstained biological molecules. Q Rev Biophys 28(2):171-193
    • (1995) Q Rev Biophys , vol.28 , Issue.2 , pp. 171-193
    • Henderson, R.1
  • 46
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 47
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B (1991) Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11(4):281-296
    • (1991) Proteins , vol.11 , Issue.4 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 48
    • 0000328844 scopus 로고
    • A new vertex algorithm to calculate solvent accessible surface-areas
    • Sridharan S, Nicholls A, Honig B (1992) A new vertex algorithm to calculate solvent accessible surface-areas. FASEB J 6(1):A174.
    • (1992) FASEB J , vol.6 , Issue.1
    • Sridharan, S.1    Nicholls, A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.