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Volumn 512, Issue 7513, 2014, Pages 166-170

Three-dimensional structure of human γ-secretase

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA GLUTAMYL HYDROLASE; GAMMA SECRETASE; NICASTRIN;

EID: 84904560883     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13567     Document Type: Article
Times cited : (288)

References (60)
  • 1
    • 35348860241 scopus 로고    scopus 로고
    • Presenilin: Running with scissors in the membrane
    • Selkoe, D. J. & Wolfe, M. S. Presenilin: running with scissors in the membrane. Cell 131, 215-221 (2007).
    • (2007) Cell , vol.131 , pp. 215-221
    • Selkoe, D.J.1    Wolfe, M.S.2
  • 2
    • 84863939887 scopus 로고    scopus 로고
    • Presenilins and γ-secretase: Structure, function, and role in Alzheimer disease
    • De Strooper, B., Iwatsubo, T. & Wolfe, M. S. Presenilins and γ-secretase: structure, function, and role in Alzheimer disease. Cold Spring Harb. Persp. Medi. 2, a006304 (2012).
    • (2012) Cold Spring Harb. Persp. Medi. , vol.2
    • De Strooper, B.1    Iwatsubo, T.2    Wolfe, M.S.3
  • 3
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391-398 (2000).
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 4
    • 84885097856 scopus 로고    scopus 로고
    • Toward the structure of presenilin/c-secretase and presenilin homologs
    • Wolfe, M. S. Toward the structure of presenilin/c-secretase and presenilin homologs. Biochim. Biophys. Acta 1828, 2886-2897 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2886-2897
    • Wolfe, M.S.1
  • 5
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-secretase complex
    • De Strooper, B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-secretase complex. Neuron 38, 9-12 (2003).
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 6
    • 0038652102 scopus 로고    scopus 로고
    • γ-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2
    • Kimberly, W. T. et al. γ-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2. Proc. Natl Acad. Sci. USA 100, 6382-6387 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6382-6387
    • Kimberly, W.T.1
  • 7
    • 84891836688 scopus 로고    scopus 로고
    • The role of protein glycosylation in Alzheimer disease
    • Schedin-Weiss,S., Winblad, B. & Tjernberg, L. O. The role of protein glycosylation in Alzheimer disease. FEBS J. 281, 46-62 (2014).
    • (2014) FEBS J. , vol.281 , pp. 46-62
    • Schedin-Weiss, S.1    Winblad, B.2    Tjernberg, L.O.3
  • 8
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 9
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1
  • 10
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like proteasemediates release of Notch intracellular domain
    • De Strooper, B. et al. A presenilin-1-dependent γ-secretase-like proteasemediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1
  • 11
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Struhl, G. & Greenwald, I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398, 522-525 (1999).
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 12
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran, G. et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190 (1996).
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1
  • 13
    • 0037468759 scopus 로고    scopus 로고
    • The role of presenilin cofactors in the γ-secretase complex
    • Takasugi, N. et al. The role of presenilin cofactors in the γ-secretase complex. Nature 422, 438-441 (2003).
    • (2003) Nature , vol.422 , pp. 438-441
    • Takasugi, N.1
  • 14
    • 0037470037 scopus 로고    scopus 로고
    • APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin?nicastrin complexes
    • Gu, Y. et al. APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin?nicastrin complexes. J. Biol. Chem. 278, 7374-7380 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 7374-7380
    • Gu, Y.1
  • 15
    • 0141733241 scopus 로고    scopus 로고
    • Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin
    • LaVoie, M. J. et al. Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin. J. Biol. Chem. 278, 37213-37222 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 37213-37222
    • Lavoie, M.J.1
  • 16
    • 58049193592 scopus 로고    scopus 로고
    • Chemical cross-linking provides a model of the γ-secretase complex subunit architecture and evidence for close proximity of the C-terminal fragment of presenilin with APH-1
    • Steiner, H., Winkler, E. & Haass, C. Chemical cross-linking provides a model of the γ-secretase complex subunit architecture and evidence for close proximity of the C-terminal fragment of presenilin with APH-1. J. Biol. Chem. 283, 34677-34686 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 34677-34686
    • Steiner, H.1    Winkler, E.2    Haass, C.3
  • 17
    • 11244272819 scopus 로고    scopus 로고
    • The presenilin C-terminus is required for ER-retention, nicastrinbinding and γ-secretase activity
    • Kaether, C. et al. The presenilin C-terminus is required for ER-retention, nicastrinbinding and γ-secretase activity. EMBO J. 23, 4738-4748 (2004).
    • (2004) EMBO J. , vol.23 , pp. 4738-4748
    • Kaether, C.1
  • 18
    • 23744491374 scopus 로고    scopus 로고
    • Nicastrin functions as a γ-secretase-substrate receptor
    • Shah, S. et al. Nicastrin functions as a γ-secretase-substrate receptor. Cell 122, 435-447 (2005).
    • (2005) Cell , vol.122 , pp. 435-447
    • Shah, S.1
  • 19
    • 70350353076 scopus 로고    scopus 로고
    • Glu-333 of nicastrin directly participates in γ-secretase activity
    • Dries, D. R. et al. Glu-333 of nicastrin directly participates in γ-secretase activity. J. Biol. Chem. 284, 29714-29724 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 29714-29724
    • Dries, D.R.1
  • 20
    • 33646483640 scopus 로고    scopus 로고
    • Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores
    • Lazarov, V. K. et al. Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores. Proc. Natl Acad. Sci. USA 103, 6889-6894 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6889-6894
    • Lazarov, V.K.1
  • 21
    • 33645116480 scopus 로고    scopus 로고
    • Three-dimensional structure of the γ-secretase complex
    • corrigendum 345, 543 (2006)
    • Ogura, T. et al. Three-dimensional structure of the γ-secretase complex. Biochem. Biophys. Res. Commun. 343, 525-534 (2006); corrigendum 345, 543 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 525-534
    • Ogura, T.1
  • 22
    • 58149094674 scopus 로고    scopus 로고
    • Cryoelectron microscopy structure of purified γ-secretase at 12A° resolution
    • Osenkowski, P. et al. Cryoelectron microscopy structure of purified γ-secretase at 12A° resolution. J. Mol. Biol. 385, 642-652 (2009).
    • (2009) J. Mol. Biol. , vol.385 , pp. 642-652
    • Osenkowski, P.1
  • 23
    • 79958718948 scopus 로고    scopus 로고
    • Structure of γ-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy
    • Renzi, F. et al. Structure of γ-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy. J. Biol. Chem. 286, 21440-21449 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 21440-21449
    • Renzi, F.1
  • 24
    • 84891889942 scopus 로고    scopus 로고
    • Structural interactions between inhibitor andsubstrate docking sites give insight intomechanismsof human PS1complexes
    • Li, Y. et al. Structural interactions between inhibitor andsubstrate docking sites give insight intomechanismsof human PS1complexes. Structure 22, 125-135 (2014).
    • (2014) Structure , vol.22 , pp. 125-135
    • Li, Y.1
  • 25
    • 77953113485 scopus 로고    scopus 로고
    • Structural investigation of the C-terminal catalytic fragment of presenilin 1
    • Sobhanifar, S. et al. Structural investigation of the C-terminal catalytic fragment of presenilin 1. Proc. Natl Acad. Sci. USA 107, 9644-9649 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9644-9649
    • Sobhanifar, S.1
  • 26
    • 84871725890 scopus 로고    scopus 로고
    • Structure of a presenilin family intramembrane aspartate protease
    • Li, X. et al. Structure of a presenilin family intramembrane aspartate protease. Nature 493, 56-61 (2013).
    • (2013) Nature , vol.493 , pp. 56-61
    • Li, X.1
  • 27
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai, X. C., Fernandez, I. S., McMullan, G. & Scheres, S. H. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. eLife 2, e00461 (2013).
    • (2013) ELife , vol.2
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.4
  • 28
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic- resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable nearatomic- resolution single-particle cryo-EM. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 29
    • 84897000112 scopus 로고    scopus 로고
    • Structure of the yeast mitochondrial large ribosomal subunit
    • Amunts, A. et al. Structure of the yeast mitochondrial large ribosomal subunit. Science 343, 1485-1489 (2014).
    • (2014) Science , vol.343 , pp. 1485-1489
    • Amunts, A.1
  • 30
    • 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, D. J., McMullan, G., Kuhlbrandt, W. & Vonck, J. Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector. eLife 3, e01963 (2014).
    • (2014) ELife , vol.3
    • Allegretti, M.1    Mills, D.J.2    McMullan, G.3    Kuhlbrandt, W.4    Vonck, J.5
  • 31
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 32
    • 13444268952 scopus 로고    scopus 로고
    • Differential contribution of the three Aph1 genes to γ-secretase activity in vivo
    • Serneels, L. et al. Differential contribution of the three Aph1 genes to γ-secretase activity in vivo. Proc. Natl Acad. Sci. USA 102, 1719-1724 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1719-1724
    • Serneels, L.1
  • 34
    • 0343819757 scopus 로고    scopus 로고
    • Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state
    • Li, Y. M. et al. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA 97, 6138-6143 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.M.1
  • 35
    • 0038607066 scopus 로고    scopus 로고
    • Differential effects of inhibitors on the γ-secretase complex. Mechanistic implications
    • Kornilova, A. Y., Das, C. & Wolfe, M. S. Differential effects of inhibitors on the γ-secretase complex. Mechanistic implications. J. Biol. Chem. 278, 16470-16473 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16470-16473
    • Kornilova, A.Y.1    Das, C.2    Wolfe, M.S.3
  • 36
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres . S, H.1
  • 37
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J.Mol. Biol. 333, 721-745 (2003).
    • (2003) J.Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 38
    • 0035312603 scopus 로고    scopus 로고
    • Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain
    • Fagan, R., Swindells, M., Overington, J. & Weir, M. Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain. Trends Biochem. Sci. 26, 213-214 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 213-214
    • Fagan, R.1    Swindells, M.2    Overington, J.3    Weir, M.4
  • 39
    • 77956444662 scopus 로고    scopus 로고
    • A remote arene-binding site on prostate specific membrane antigen revealed by antibody-recruiting small molecules
    • Zhang, A. X. et al. A remote arene-binding site on prostate specific membrane antigen revealed by antibody-recruiting small molecules. J. Am. Chem. Soc. 132, 12711-12716 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12711-12716
    • Zhang, A.X.1
  • 40
    • 79953305108 scopus 로고    scopus 로고
    • Functional and topological analysis of Pen-2, the fourth subunit of the γ-secretase complex
    • Bammens, L., Chavez-Gutierrez, L., Tolia, A., Zwijsen, A. & De Strooper, B. Functional and topological analysis of Pen-2, the fourth subunit of the γ-secretase complex. J. Biol. Chem. 286, 12271-12282 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 12271-12282
    • Bammens, L.1    Chavez-Gutierrez, L.2    Tolia, A.3    Zwijsen, A.4    De Strooper, B.5
  • 41
    • 29644432040 scopus 로고    scopus 로고
    • Pen-2 is incorporated into the γ-secretase complex through binding to transmembrane domain 4 of presenilin 1
    • Watanabe, N. et al. Pen-2 is incorporated into the γ-secretase complex through binding to transmembrane domain 4 of presenilin 1. J. Biol. Chem. 280, 41967-41975 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 41967-41975
    • Watanabe, N.1
  • 42
    • 29644435433 scopus 로고    scopus 로고
    • Evidence that the "nF"motif in transmembrane domain 4 of presenilin 1 is critical for binding with PEN-2
    • Kim, S. H. & Sisodia, S. S. Evidence that the "NF"motif in transmembrane domain 4 of presenilin 1 is critical for binding with PEN-2. J. Biol. Chem. 280, 41953-41966 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 41953-41966
    • Kim, S.H.1    Sisodia, S.S.2
  • 43
    • 81255210901 scopus 로고    scopus 로고
    • Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
    • Althoff, T., Mills, D. J., Popot, J. L. & Kuhlbrandt, W. Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J. 30, 4652-4664 (2011).
    • (2011) EMBO J. , vol.30 , pp. 4652-4664
    • Althoff, T.1    Mills, D.J.2    Popot, J.L.3    Kuhlbrandt, W.4
  • 44
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • Tribet, C., Audebert, R. & Popot, J. L. Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc. Natl Acad. Sci. USA 93, 15047-15050 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.L.3
  • 45
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Published online 2006 Oct 11
    • Wang, Y., Zhang, Y. & Ha, Y. Crystal structure of a rhomboid family intramembrane protease. Nature 444, 179-180 (2006). Published online 2006 Oct 11.
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 46
    • 33845365770 scopus 로고    scopus 로고
    • Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry
    • Wu, Z. et al. Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nature Struct. Mol. Biol. 13, 1084-1091 (2006).
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 1084-1091
    • Wu, Z.1
  • 47
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • Ben-Shem, A., Fass, D. & Bibi, E. Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc. Natl Acad. Sci. USA 104, 462-466 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 48
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • Feng, L. et al. Structure of a site-2 protease family intramembrane metalloprotease. Science 318, 1608-1612 (2007).
    • (2007) Science , vol.318 , pp. 1608-1612
    • Feng, L.1
  • 50
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 51
    • 0347089037 scopus 로고    scopus 로고
    • Electroporation and RNA interference in the rodent retina in vivo and in vitro
    • Matsuda, T. & Cepko, C. L. Electroporation and RNA interference in the rodent retina in vivo and in vitro. Proc. Natl Acad. Sci. USA 101, 16-22 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 16-22
    • Matsuda, T.1    Cepko, C.L.2
  • 52
    • 5644288963 scopus 로고    scopus 로고
    • A facile method for high-throughput co-expression of protein pairs
    • Alexandrov, A. et al. A facile method for high-throughput co-expression of protein pairs. Mol. Cell. Proteomics 3, 934-938 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 934-938
    • Alexandrov, A.1
  • 54
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determinationof local defocus and specimen tilt in electron microscopy
    • Mindell, J. A. & Grigorieff, N. Accurate determinationof local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 55
    • 84881432897 scopus 로고    scopus 로고
    • PRIME: Probabilistic initial 3D model generation for single-particle cryo-electron microscopy
    • Elmlund, H., Elmlund, D. & Bengio, S. PRIME: probabilistic initial 3D model generation for single-particle cryo-electron microscopy. Structure 21, 1299-1306 (2013).
    • (2013) Structure , vol.21 , pp. 1299-1306
    • Elmlund, H.1    Elmlund, D.2    Bengio, S.3
  • 56
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013).
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 57
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63-65 (2014).
    • (2014) Nature Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 59
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1


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