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Volumn 113, Issue 12, 2016, Pages 3245-3250

Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance

Author keywords

Cryo EM; Evolutionary covariance; Structure; V ATPase; V A ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84962228587     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1521990113     Document Type: Article
Times cited : (43)

References (66)
  • 1
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac M (2007) Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology. Nat Rev Mol Cell Biol 8(11):917-929.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.11 , pp. 917-929
    • Forgac, M.1
  • 2
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar proton pump
    • Blair HC, Teitelbaum SL, Ghiselli R, Gluck S (1989) Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 245(4920):855-857.
    • (1989) Science , vol.245 , Issue.4920 , pp. 855-857
    • Blair, H.C.1    Teitelbaum, S.L.2    Ghiselli, R.3    Gluck, S.4
  • 3
    • 4644245032 scopus 로고    scopus 로고
    • Renal vacuolar H+-ATPase
    • Wagner CA, et al. (2004) Renal vacuolar H+-ATPase. Physiol Rev 84(4):1263-1314.
    • (2004) Physiol Rev , vol.84 , Issue.4 , pp. 1263-1314
    • Wagner, C.A.1
  • 4
    • 0033946477 scopus 로고    scopus 로고
    • Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis
    • Frattini A, et al. (2000) Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis. Nat Genet 25(3): 343-346.
    • (2000) Nat Genet , vol.25 , Issue.3 , pp. 343-346
    • Frattini, A.1
  • 5
    • 0032943534 scopus 로고    scopus 로고
    • Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness
    • Karet FE, et al. (1999) Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness. Nat Genet 21(1):84-90.
    • (1999) Nat Genet , vol.21 , Issue.1 , pp. 84-90
    • Karet, F.E.1
  • 6
    • 0033812944 scopus 로고    scopus 로고
    • Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing
    • Smith AN, et al. (2000) Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing. Nat Genet 26(1):71-75.
    • (2000) Nat Genet , vol.26 , Issue.1 , pp. 71-75
    • Smith, A.N.1
  • 7
    • 67650236818 scopus 로고    scopus 로고
    • Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells
    • Hinton A, et al. (2009) Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells. J Biol Chem 284(24):16400-16408.
    • (2009) J Biol Chem , vol.284 , Issue.24 , pp. 16400-16408
    • Hinton, A.1
  • 8
    • 84929335211 scopus 로고    scopus 로고
    • Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
    • Zhao J, Benlekbir S, Rubinstein JL (2015) Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase. Nature 521(7551):241-245.
    • (2015) Nature , vol.521 , Issue.7551 , pp. 241-245
    • Zhao, J.1    Benlekbir, S.2    Rubinstein, J.L.3
  • 9
    • 84855793968 scopus 로고    scopus 로고
    • Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase
    • Lau WCY, Rubinstein JL (2012) Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase. Nature 481(7380):214-218.
    • (2012) Nature , vol.481 , Issue.7380 , pp. 214-218
    • Lau, W.C.Y.1    Rubinstein, J.L.2
  • 10
    • 77949269543 scopus 로고    scopus 로고
    • The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase
    • Lee LK, Stewart AG, Donohoe M, Bernal RA, Stock D (2010) The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase. Nat Struct Mol Biol 17(3):373-378.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.3 , pp. 373-378
    • Lee, L.K.1    Stewart, A.G.2    Donohoe, M.3    Bernal, R.A.4    Stock, D.5
  • 11
    • 84868582759 scopus 로고    scopus 로고
    • Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex
    • Oot RA, Huang LS, Berry EA, Wilkens S (2012) Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex. Structure 20(11): 1881-1892.
    • (2012) Structure , vol.20 , Issue.11 , pp. 1881-1892
    • Oot, R.A.1    Huang, L.S.2    Berry, E.A.3    Wilkens, S.4
  • 12
    • 84879955381 scopus 로고    scopus 로고
    • Origin of asymmetry at the intersubunit interfaces of V1-ATPase from Thermus thermophilus
    • Nagamatsu Y, Takeda K, Kuranaga T, Numoto N, Miki K (2013) Origin of asymmetry at the intersubunit interfaces of V1-ATPase from Thermus thermophilus. J Mol Biol 425(15):2699-2708.
    • (2013) J Mol Biol , vol.425 , Issue.15 , pp. 2699-2708
    • Nagamatsu, Y.1    Takeda, K.2    Kuranaga, T.3    Numoto, N.4    Miki, K.5
  • 13
    • 9144222170 scopus 로고    scopus 로고
    • Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase
    • Iwata M, et al. (2004) Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase. Proc Natl Acad Sci USA 101(1):59-64.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.1 , pp. 59-64
    • Iwata, M.1
  • 14
    • 17844369968 scopus 로고    scopus 로고
    • Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae
    • Murata T, Yamato I, Kakinuma Y, Leslie AG, Walker JE (2005) Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science 308(5722):654-659.
    • (2005) Science , vol.308 , Issue.5722 , pp. 654-659
    • Murata, T.1    Yamato, I.2    Kakinuma, Y.3    Leslie, A.G.4    Walker, J.E.5
  • 15
    • 84860388832 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase
    • Srinivasan S, Vyas NK, Baker ML, Quiocho FA (2011) Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase. J Mol Biol 412(1):14-21.
    • (2011) J Mol Biol , vol.412 , Issue.1 , pp. 14-21
    • Srinivasan, S.1    Vyas, N.K.2    Baker, M.L.3    Quiocho, F.A.4
  • 16
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge W, Lill H, Engelbrecht S (1997) ATP synthase: An electrochemical transducer with rotatory mechanics. Trends Biochem Sci 22(11):420-423.
    • (1997) Trends Biochem Sci , vol.22 , Issue.11 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 17
    • 0027970177 scopus 로고
    • A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit
    • Vik SB, Antonio BJ (1994) A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit. J Biol Chem 269(48):30364-30369.
    • (1994) J Biol Chem , vol.269 , Issue.48 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 18
    • 76549094484 scopus 로고    scopus 로고
    • Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor
    • Lau WCY, Rubinstein JL (2010) Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor. Proc Natl Acad Sci USA 107(4):1367-1372.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.4 , pp. 1367-1372
    • Lau, W.C.Y.1    Rubinstein, J.L.2
  • 19
    • 84927628815 scopus 로고    scopus 로고
    • Horizontal membrane-intrinsic α-helices in the stator asubunit of an F-type ATP synthase
    • Allegretti M, et al. (2015) Horizontal membrane-intrinsic α-helices in the stator asubunit of an F-type ATP synthase. Nature 521(7551):237-240.
    • (2015) Nature , vol.521 , Issue.7551 , pp. 237-240
    • Allegretti, M.1
  • 20
    • 84949921757 scopus 로고    scopus 로고
    • Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
    • Zhou A, et al. (2015) Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. eLife 4:e10180.
    • (2015) ELife , vol.4 , pp. e10180
    • Zhou, A.1
  • 21
    • 84945582226 scopus 로고    scopus 로고
    • Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution
    • Morales-Rios E, Montgomery MG, Leslie AGW, Walker JE (2015) Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution. Proc Natl Acad Sci USA 112(43):13231-13236.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.43 , pp. 13231-13236
    • Morales-Rios, E.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 22
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Göbel U, Sander C, Schneider R, Valencia A (1994) Correlated mutations and residue contacts in proteins. Proteins 18(4):309-317.
    • (1994) Proteins , vol.18 , Issue.4 , pp. 309-317
    • Göbel, U.1    Sander, C.2    Schneider, R.3    Valencia, A.4
  • 23
    • 0027465713 scopus 로고
    • Modeling of transmembrane seven helix bundles
    • Cronet P, Sander C, Vriend G (1993) Modeling of transmembrane seven helix bundles. Protein Eng 6(1):59-64.
    • (1993) Protein Eng , vol.6 , Issue.1 , pp. 59-64
    • Cronet, P.1    Sander, C.2    Vriend, G.3
  • 24
    • 84862647180 scopus 로고    scopus 로고
    • Three-dimensional structures of membrane proteins from genomic sequencing
    • Hopf TA, et al. (2012) Three-dimensional structures of membrane proteins from genomic sequencing. Cell 149(7):1607-1621.
    • (2012) Cell , vol.149 , Issue.7 , pp. 1607-1621
    • Hopf, T.A.1
  • 25
    • 84899847547 scopus 로고    scopus 로고
    • Robust and accurate prediction of residue- residue interactions across protein interfaces using evolutionary information
    • Ovchinnikov S, Kamisetty H, Baker D (2014) Robust and accurate prediction of residue- residue interactions across protein interfaces using evolutionary information. eLife 3:e02030.
    • (2014) ELife , vol.3 , pp. e02030
    • Ovchinnikov, S.1    Kamisetty, H.2    Baker, D.3
  • 26
    • 84855793968 scopus 로고    scopus 로고
    • Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase
    • Lau WCY, Rubinstein JL (2012) Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase. Nature 481(7380):214-218.
    • (2012) Nature , vol.481 , Issue.7380 , pp. 214-218
    • Lau, W.C.Y.1    Rubinstein, J.L.2
  • 27
    • 84947545693 scopus 로고    scopus 로고
    • Validating maps from single particle electron cryomicroscopy
    • Rosenthal PB, Rubinstein JL (2015) Validating maps from single particle electron cryomicroscopy. Curr Opin Struct Biol 34:135-144.
    • (2015) Curr Opin Struct Biol , vol.34 , pp. 135-144
    • Rosenthal, P.B.1    Rubinstein, J.L.2
  • 28
    • 84922021496 scopus 로고    scopus 로고
    • Vma9p need not be associated with the yeast V-ATPase for fully-coupled proton pumping activity in vitro
    • Bueler SA, Rubinstein JL (2015) Vma9p need not be associated with the yeast V-ATPase for fully-coupled proton pumping activity in vitro. Biochemistry 54(3):853-858.
    • (2015) Biochemistry , vol.54 , Issue.3 , pp. 853-858
    • Bueler, S.A.1    Rubinstein, J.L.2
  • 29
    • 34250886311 scopus 로고    scopus 로고
    • Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria
    • Chen R, Runswick MJ, Carroll J, Fearnley IM, Walker JE (2007) Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria. FEBS Lett 581(17):3145-3148.
    • (2007) FEBS Lett , vol.581 , Issue.17 , pp. 3145-3148
    • Chen, R.1    Runswick, M.J.2    Carroll, J.3    Fearnley, I.M.4    Walker, J.E.5
  • 30
    • 35448937657 scopus 로고    scopus 로고
    • Identification of membrane proteins by tandem mass spectrometry of protein ions
    • Carroll J, Altman MC, Fearnley IM, Walker JE (2007) Identification of membrane proteins by tandem mass spectrometry of protein ions. Proc Natl Acad Sci USA 104(36):14330-14335.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.36 , pp. 14330-14335
    • Carroll, J.1    Altman, M.C.2    Fearnley, I.M.3    Walker, J.E.4
  • 31
    • 80053413602 scopus 로고    scopus 로고
    • Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase
    • Toei M, Toei S, Forgac M (2011) Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase. J Biol Chem 286(40):35176-35186.
    • (2011) J Biol Chem , vol.286 , Issue.40 , pp. 35176-35186
    • Toei, M.1    Toei, S.2    Forgac, M.3
  • 32
    • 68949187842 scopus 로고    scopus 로고
    • Refinement of protein structures into low-resolution density maps using rosetta
    • DiMaio F, Tyka MD, Baker ML, Chiu W, Baker D (2009) Refinement of protein structures into low-resolution density maps using rosetta. J Mol Biol 392(1):181-190.
    • (2009) J Mol Biol , vol.392 , Issue.1 , pp. 181-190
    • DiMaio, F.1    Tyka, M.D.2    Baker, M.L.3    Chiu, W.4    Baker, D.5
  • 34
    • 0035940474 scopus 로고    scopus 로고
    • Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
    • Kawasaki-Nishi S, Nishi T, Forgac M (2001) Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation. Proc Natl Acad Sci USA 98(22): 12397-12402.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.22 , pp. 12397-12402
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 35
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo
    • Kane PM (1995) Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo. J Biol Chem 270(28):17025-17032.
    • (1995) J Biol Chem , vol.270 , Issue.28 , pp. 17025-17032
    • Kane, P.M.1
  • 36
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner JP, et al. (1995) Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J Biol Chem 270(10):5649-5653.
    • (1995) J Biol Chem , vol.270 , Issue.10 , pp. 5649-5653
    • Sumner, J.P.1
  • 37
    • 0028224791 scopus 로고
    • STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p
    • Manolson MF, et al. (1994) STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p. J Biol Chem 269(19):14064-14074.
    • (1994) J Biol Chem , vol.269 , Issue.19 , pp. 14064-14074
    • Manolson, M.F.1
  • 38
    • 0033591450 scopus 로고    scopus 로고
    • Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase
    • Leng XH, Nishi T, Forgac M (1999) Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase. J Biol Chem 274(21):14655-14661.
    • (1999) J Biol Chem , vol.274 , Issue.21 , pp. 14655-14661
    • Leng, X.H.1    Nishi, T.2    Forgac, M.3
  • 39
    • 51049099817 scopus 로고    scopus 로고
    • Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification
    • Wang Y, Toei M, Forgac M (2008) Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification. J Biol Chem 283(30):20696-20702.
    • (2008) J Biol Chem , vol.283 , Issue.30 , pp. 20696-20702
    • Wang, Y.1    Toei, M.2    Forgac, M.3
  • 40
    • 0029831620 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase
    • Leng XH, Manolson MF, Liu Q, Forgac M (1996) Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase. J Biol Chem 271(37):22487-22493.
    • (1996) J Biol Chem , vol.271 , Issue.37 , pp. 22487-22493
    • Leng, X.H.1    Manolson, M.F.2    Liu, Q.3    Forgac, M.4
  • 41
    • 0032549629 scopus 로고    scopus 로고
    • Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase
    • Leng XH, Manolson MF, Forgac M (1998) Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase. J Biol Chem 273(12):6717-6723.
    • (1998) J Biol Chem , vol.273 , Issue.12 , pp. 6717-6723
    • Leng, X.H.1    Manolson, M.F.2    Forgac, M.3
  • 42
    • 0142149158 scopus 로고    scopus 로고
    • Interacting helical surfaces of the transmembrane segments of subunits a and c′ of the yeast V-ATPase defined by disulfidemediated cross-linking
    • Kawasaki-Nishi S, Nishi T, Forgac M (2003) Interacting helical surfaces of the transmembrane segments of subunits a and c′ of the yeast V-ATPase defined by disulfidemediated cross-linking. J Biol Chem 278(43):41908-41913.
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 41908-41913
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 43
    • 33751085062 scopus 로고    scopus 로고
    • A model for the proteolipid ring and bafilomycin/concanamycin-binding site in the vacuolar ATPase of Neurospora crassa
    • Bowman BJ, McCall ME, Baertsch R, Bowman EJ (2006) A model for the proteolipid ring and bafilomycin/concanamycin-binding site in the vacuolar ATPase of Neurospora crassa. J Biol Chem281(42):31885-31893.
    • (2006) J Biol Chem , vol.281 , Issue.42 , pp. 31885-31893
    • Bowman, B.J.1    McCall, M.E.2    Baertsch, R.3    Bowman, E.J.4
  • 44
    • 28844433952 scopus 로고    scopus 로고
    • Subunit a of the yeast V-ATPase participates in binding of bafilomycin
    • Wang Y, Inoue T, Forgac M (2005) Subunit a of the yeast V-ATPase participates in binding of bafilomycin. J Biol Chem 280(49):40481-40488.
    • (2005) J Biol Chem , vol.280 , Issue.49 , pp. 40481-40488
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 45
    • 0028880405 scopus 로고
    • The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity
    • Hatch LP, Cox GB, Howitt SM (1995) The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity. J Biol Chem 270(49):29407-29412.
    • (1995) J Biol Chem , vol.270 , Issue.49 , pp. 29407-29412
    • Hatch, L.P.1    Cox, G.B.2    Howitt, S.M.3
  • 46
    • 84867664688 scopus 로고    scopus 로고
    • Structural differences between thermophilic and mesophilic membrane proteins
    • Meruelo AD, Han SK, Kim S, Bowie JU (2012) Structural differences between thermophilic and mesophilic membrane proteins. Protein Sci 21(11):1746-1753.
    • (2012) Protein Sci , vol.21 , Issue.11 , pp. 1746-1753
    • Meruelo, A.D.1    Han, S.K.2    Kim, S.3    Bowie, J.U.4
  • 47
    • 0023895368 scopus 로고
    • Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli
    • Cain BD, Simoni RD (1988) Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli. J Biol Chem 263(14):6606-6612.
    • (1988) J Biol Chem , vol.263 , Issue.14 , pp. 6606-6612
    • Cain, B.D.1    Simoni, R.D.2
  • 48
    • 0142211194 scopus 로고    scopus 로고
    • Subunit arrangement in V-ATPase from Thermus thermophilus
    • Yokoyama K, et al. (2003) Subunit arrangement in V-ATPase from Thermus thermophilus. J Biol Chem 278(43):42686-42691.
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 42686-42691
    • Yokoyama, K.1
  • 49
    • 84891001553 scopus 로고    scopus 로고
    • Fabrication of carbon films with ∼ 500 nm holes for cryo-EM with a direct detector device
    • Marr CR, Benlekbir S, Rubinstein JL (2014) Fabrication of carbon films with ∼ 500 nm holes for cryo-EM with a direct detector device. J Struct Biol 185(1):42-47.
    • (2014) J Struct Biol , vol.185 , Issue.1 , pp. 42-47
    • Marr, C.R.1    Benlekbir, S.2    Rubinstein, J.L.3
  • 50
  • 51
    • 84946473054 scopus 로고    scopus 로고
    • Alignment of cryo-EM movies of individual particles by optimization of image translations
    • Rubinstein JL, Brubaker MA (2015) Alignment of cryo-EM movies of individual particles by optimization of image translations. J Struct Biol 192(2):188-195.
    • (2015) J Struct Biol , vol.192 , Issue.2 , pp. 188-195
    • Rubinstein, J.L.1    Brubaker, M.A.2
  • 52
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142(3):334-347.
    • (2003) J Struct Biol , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 53
    • 84873999666 scopus 로고    scopus 로고
    • TMaCS: A hybrid template matching and classification system for partially-automated particle selection
    • Zhao J, Brubaker MA, Rubinstein JL (2013) TMaCS: A hybrid template matching and classification system for partially-automated particle selection. J Struct Biol 181(3): 234-242.
    • (2013) J Struct Biol , vol.181 , Issue.3 , pp. 234-242
    • Zhao, J.1    Brubaker, M.A.2    Rubinstein, J.L.3
  • 54
    • 84946486192 scopus 로고    scopus 로고
    • Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images
    • Zhao J, Brubaker MA, Benlekbir S, Rubinstein JL (2015) Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images. J Struct Biol 192(2):209-215.
    • (2015) J Struct Biol , vol.192 , Issue.2 , pp. 209-215
    • Zhao, J.1    Brubaker, M.A.2    Benlekbir, S.3    Rubinstein, J.L.4
  • 55
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SHW (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.W.1
  • 56
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard TD, Huang CC, Ferrin TE (2007) Visualizing density maps with UCSF Chimera. J Struct Biol 157(1):281-287.
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 57
    • 84863955498 scopus 로고    scopus 로고
    • Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM
    • Baker LA, Watt IN, Runswick MJ, Walker JE, Rubinstein JL (2012) Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM. Proc Natl Acad Sci USA 109(29):11675-11680.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.29 , pp. 11675-11680
    • Baker, L.A.1    Watt, I.N.2    Runswick, M.J.3    Walker, J.E.4    Rubinstein, J.L.5
  • 58
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo- em density maps
    • Kucukelbir A, Sigworth FJ, Tagare HD (2014) Quantifying the local resolution of cryo- EM density maps. Nat Methods 11(1):63-65.
    • (2014) Nat Methods , vol.11 , Issue.1 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 59
    • 84930074657 scopus 로고    scopus 로고
    • The Phyre2 web portal for protein modeling, prediction and analysis
    • Kelley LA, Mezulis S, Yates CM, Wass MN, Sternberg MJ (2015) The Phyre2 web portal for protein modeling, prediction and analysis. Nat Protoc 10(6):845-858.
    • (2015) Nat Protoc , vol.10 , Issue.6 , pp. 845-858
    • Kelley, L.A.1    Mezulis, S.2    Yates, C.M.3    Wass, M.N.4    Sternberg, M.J.5
  • 60
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco LG, Villa E, Mitra K, Frank J, Schulten K (2008) Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16(5): 673-683.
    • (2008) Structure , vol.16 , Issue.5 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 61
    • 42649144152 scopus 로고    scopus 로고
    • Angle determination for side views in single particle electron microscopy
    • Baker LA, Rubinstein JL (2008) Angle determination for side views in single particle electron microscopy. J Struct Biol 162:260-270.
    • (2008) J Struct Biol , vol.162 , pp. 260-270
    • Baker, L.A.1    Rubinstein, J.L.2
  • 62
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745.
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 63
    • 82855163967 scopus 로고    scopus 로고
    • Protein 3D structure computed from evolutionary sequence variation
    • Marks DS, et al. (2011) Protein 3D structure computed from evolutionary sequence variation. PLoS One 6:e28766.
    • (2011) PLoS One , vol.6 , pp. e28766
    • Marks, D.S.1
  • 64
    • 67649472570 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction using support vector machines
    • Nugent T, Jones DT (2009) Transmembrane protein topology prediction using support vector machines. BMC Bioinformatics 10:159.
    • (2009) BMC Bioinformatics , vol.10 , pp. 159
    • Nugent, T.1    Jones, D.T.2
  • 65
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F, et al. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7:539.
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1
  • 66
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Ch 5: Unit 5.6
    • Eswar N, et al. (2006) Comparative protein structure modeling using Modeller. Curr Protoc Bioinformatics Ch 5:Unit 5.6.
    • (2006) Curr Protoc Bioinformatics
    • Eswar, N.1


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