1. Y. Norimatsu, K. Hasegawa, N. Shimizu and C.Toyoshima: Protein–phospholipid interplay revealed with crystals of a calcium pump, Nature, 545, 193-198 (2017)
2. SI. Yonekura, C.Toyoshima: Mn²⁺ transport by Ca²⁺-ATPase of sarcoplasmic reticulum. FEBS Letters, 590, 2086–2095 (2016)
3. C.Toyoshima: The road to understanding an ion pump, PHYSICA SCRIPTA, 91, 042501 (2016)
4. Y. Zhao, H. Ogawa, SI. Yonekura, H. Mitsuhashi, S. Mitsuhashi, I. Nishimo, C.Toyoshima, S. Ishiura: Functional analysis of SERCA1b, a highly expressed SERCA1 variant in myotonic dystrophy type 1 muscle BBA-MOLECULAR BASIS OF DISEASE 1852,2042-2047 (2015)
5. H. Ogawa, F.Cornelius, A. Hirata and C.Toyoshima: Sequential substitution of K⁺ bound to Na⁺,K⁺-ATPase visualised by X-ray crystallography. Nature Commun, 6: 8004 (2015)
6. F. Cornelius, M. Habeck, R. Kanai, C.Toyoshima and S.J.D. Karlish: General and specific lipid–protein interactions in Na,K-ATPase. Biochim. Biophys. Acta. 1848, 1729-1743 (2015)
7. M.Morita, H. Ogawa, O. Ohno, T. Yamori, K. Suenaga, C. Toyoshima: Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca²⁺pumps with a unique mode of binding. FEBS Letters 589, 1406–1411 (201)
8. K. Yonekura, K. Kato, M. Ogasawara, M. Tomita and C.Toyoshima: Electron crystallography of ultrathin 3D protein crystals: Atomic models with charges.: Proc. Nat. Acad. Sci. USA. 112, 3368-3373 (2015) doi:10.1073/pnas.1500724112
9. M. Habeck, H. Haviv,A. Katz, E. Kapri-Pardes, S. Ayciriex, A. Shevchenko,H. Ogawa,C.Toyoshima and S.J.D. Karlish: Stimulation, inhibition or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites. J. Biol. Chem. 290, 4829-4842 (2015) doi: 10.1074/jbc.M114.611384
10. T. Sakai, Y. Matsumoto, M. Ishikawa, K. Sugita, Y. Hashimoto, N. Wakai, A. Kitao, E. Morishita, C.Toyoshima, T. Hayashi, T. Akiyama: Design, synthesis and structure-activity relationship studies of novel sirtuin 2 (SIRT2) inhibitors with a benzamide skeleton: Bioorg. Med. Chem. 23, 328-339 (2015)
11. H. Takai, K. Masuda, T. Sato, Y. Sakaguchi, T. Suzuki, T. Suzuki, R. Koyama-Nasu, Y. Nasu-Nishimura, Y. Katou, H. Ogawa, Y. Morishita, H. Kozuka-Hata, M. Oyama, T. Todo, Y. Ino,  A. Mukasa, N. Siato, C.Toyoshima, K. Shirahige and T. Akiyama: 5-Hydroxylmethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex.. Cell reports doi: 10.1016/j.celrep.2014.08.071
12. Y. Akai, R. Kanai, N. Nakazawa, M. Ebe, C.Toyoshima and M. Yanagida: ATPase-dependent auto-phosphorylation of the open condensin hinge diminishes DNA binding. Open Biol. 4, 140193 (2014) doi: 10.1098/rsob.140193.
13. R. Kanai, H. Ogawa, B. Vilsen, F. Cornelius, C.Toyoshima, Crystal structure of a Na⁺-bound Na⁺,K⁺-ATPase preceding the E1P state. Nature 502, 201-6 (2013) [pubmed].[PressRelease(JP)] [PressRelease(ENG)]
14. C.Toyoshima, S. Iwasawa, H. Ogawa, A. Hirata, J. Tsueda, G. Inesi: Crystal structures of the calcium pump and sarcolipin in the Mg²⁺-bound E1 state. Nature 495, 260-4 (2013) [pubmed] [PressRelease(JP)]
15. H. Haviv, M. Habeck, R.Kanai, C.Toyoshima, S.J. Karlish: Neutral phospholipids stimulate Na, K-ATPase activity: a specific lipid-protein interaction. JBC 288, 10073-81 (2013) [pubmed]
16. F. Cornelius, R. Kanai, C.Toyoshima: A structural view on the functional importance of the sugar moiety and steroid hydroxyls of cardiotonic steroids in binding to Na, K-ATPase.JBC 288, 6602-16 (2013) [pubmed]
17. N. Okamoto, H. Ogawa, C.Toyoshima: A new method for establishing stable cell lines and its use for large-scale production of human guanylyl cyclase-B receptor and of the extracellular domain..Biochem. Biophys. Res. Comm. 426, 260-5 (2012) [pubmed]
18. C.Toyoshima, R. Kanai, F. Cornelius: First crystal structures of Na⁺,K⁺-ATPase: new light on the oldest ion pump.Structure 19, 1732-8 (2011) [pubmed]
19. F. Cornelius, Y.A. Mahmmoud, C.Toyoshima: Metal fluoride complexes of Na,K-ATPase. Characterization of fluoride-stabilized phosphoenzyme analogues and their interaction with cardiotonic steroids.JBC 286, 29882-92 (2011) [pubmed]
20. C. Toyoshima, S. Yonekura, J. Tsueda, S. Iwasawa: Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca²⁺-ATPase in the absence of Ca²⁺. PNAS 108, 1833-8 (2011) [pubmed]
21. Y. Sugita, M. Ikeguchi, C. Toyoshima: Relationship between Ca²⁺-affinity and shielding of bulk water in the Ca²⁺-pump from molecular dynamics simulations.PNAS 107, 21465-9 (2010) [pubmed]
22. H. Ogawa, T. Shinoda, F. Cornelius, and C. Toyoshima: Crystal structure of the sodium-potassium pump (Na⁺,K⁺-ATPase) with bound potassium and ouabain PNAS 106, 13742-13747 (2009) [pubmed]
23. T. Shinoda, H. Ogawa, F. Cornelius and C. Toyoshima: Crystal structure of the sodium-potassium pump at 2.4 Å resolution. Nature 459, 446-450 (2009) [pubmed]
24. T. Morita, D. Hussain, M. Asahi, T. Tsuda, K. Kurzydlowski, C. Toyoshima, D. H. MacLennan: Interaction sites among phospholamban, sarcolipin, and the sarco(endo)plasmic reticulum Ca²⁺-ATPase. Biochem. Biophys. Res. Comm. 369, 188-194 (2008).[pubmed]
25. Y. Hatori, A. Hirata, C. Toyoshima, D. Lewis, R. Pilankatta, and G. Inesi: Intermediate phosphorylation reactions in the mechanism of ATP utilization by the copper ATPase (CopA) of Thermotoga maritima. J. Biol. Chem. 283, 22541-22549 (2008).[pubmed]
26. C Xu, A. M. Prasad, G. Inesi and C. Toyoshima: Critical role of Val-304 in conformational transitions that allow Ca²⁺ occlusion and phosphoenzyme turnover in the Ca²⁺ transport ATPase. J. Biol. Chem. 283, 3297-3304 (2008) [pubmed]
27. G. Inesi, D. Lewis, C. Toyoshima, A. Hirata and Leopoldo de Meis: Conformational fluctuations of the Ca²⁺-ATPase in the native membrane environment-Effects of pH, temperature, catalytic substrates, and thapsigargin. J.Biol.Chem.283, 1189-1196 (2008) [pubmed]
28. C. Montigny, M. Picard, G. Lenoir, C. Gauron, C. Toyoshima and P. Champeil: Inhibitors bound to Ca²⁺-Free sarcoplasmic reticulum Ca²⁺-ATPase lock its transmembrane region but not necessarily its cytosolic region, revealing the flexibility of the loops connecting transmembrane and cytosolic domains. Biochemistry, 46, 15162-15174 (2007) [pubmed]
29. C. Toyoshima, Y. Norimatsu, S. Iwasawa, T. Tsuda and H. Ogawa: How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proc. Nat. Acad. Sci. USA. 104, 19831-19836 (2007) [pubmed]
30. K. Yonekura, C. Toyoshima: Structure determination of tubular crystals of membrane proteins. IV. Distortion correction and its combined application with real-space averaging and solvent flattening. Ultramicroscopy, 107, 1141-1158 (2007) [pubmed]
31. Y. Hatori, E. Majima, T. Tsuda and C. Toyoshima: Domain organization and movements in heavy metal ion pumps: Papain digestion of CopA, a Cu⁺-transporting ATPase. J. Biol. Chem. 282, 25213-25221(2007) [pubmed]
32. M. Takahashi, Y. Kondou and C. Toyoshima: Interdomain communication in calcium pump as revealed in the crystalstructures with transmembrane inhibitors. Proc. Nat. Acad. Sci. USA. 104 (2007) 5800-5805. [pubmed]
33. G. Inesi, D. Lewis, H. Ma, A. Prasad and C. Toyoshima: Concerted conformational effects of Ca²⁺ and ATP are required for activation of sequential reactions in the Ca²⁺ ATPase (SERCA) catalytic cycle. Biochemistry 46 (2006) 13769-13778. [pubmed]
34. Y. Sugita, N. Miyashita, T. Yoda, M. Ikeguchi and C. Toyoshima: Structural changes of the cytoplasmic domain of phospholamban by phosphorylation at Ser16: A molecular dynamics study. Biochemistry 45 (2006) 11752-11761.[pubmed]
35. M. Picard, C. Toyoshima and P. Champeil: Effects of inhibitors on luminal opening of Ca²⁺ binding sites in an E2P-like complex of sarcoplasmic reticulum Ca²⁺-ATPase with Be²⁺-fluoride. J. Biol. Chem. 281 (2006) 3360-3369. [pubmed]
36. K. Obara, N. Miyashita, C. Xu, I. Toyoshima, Y. Sugita, G. Inesi and C. Toyoshima: Structural role of countertransport revealed in Ca²⁺ pump crystal structure in the absence of Ca²⁺. Proc. Nat. Acad. Sci. USA. 102 (2005) 14489-14496. [pubmed]
37. H. Ma, D. Lewis, C. Xu, G. Inesi and C. Toyoshima: Functional and structural roles of critical amino acids within the"N", "P", and "A" domains of the Ca²⁺ ATPase (SERCA) headpiece. Biochemistry. 44 (2005) 8090-8100. [pubmed]
38. M. Picard, C. Toyoshima and P. Champeil: The average conformation at micromolar [Ca²⁺] of Ca²⁺-ATPase with bound nucleotide differs from that adopted with the transition state analog ADP.AlFx or with AMPPCP under crystallization conditions at millimolar [Ca²⁺]. J. Biol. Chem. 280 (2005) 18745-18754. [pubmed]
39. Y. Sugita, N. Miyashita, M. Ikeguchi, A. Kidera, and C. Toyoshima: Protonation of the acidic residues in the transmembrane cation-binding sites of the Ca²⁺ pump. J. Am. Chem. Soc. 127 (2005) 6150-6151. [pubmed]
40. C. Toyoshima, H. Nomura and T. Tsuda: Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432 (2004) 361-368. [pubmed] [reprint] [Supplement]
41. C. Toyoshima and T. Mizutani: Crystal structure of the calcium pump with a bound ATP analogue. Nature 430 (2004) 529-535. [pubmed] [reprint] [Supplement]
42. C. Xu, H. Ma, G. Inesi, M.K. Al-Shawi and C. Toyoshima: Specific structural requirement for the inhibitory effect of thapsigargin on the Ca²⁺ ATPase SERCA. J. Biol. Chem. 279 (2004) 17973-17979. [pubmed]
43. M. Asahi, Y. Sugita, K. Kurzydlowski, S. D. Leon, M. Tada, C. Toyoshima, and D.H. MacLennan: Sarcolipin regulates sarco(endo)plasmic reticulum Ca²⁺-ATPase(SERCA) by binding to transmembrane helices alone or in association with phospholamban. Proc. Nat. Acad. Sci. USA. 100 (2003) 5040-5045. [pubmed]
44. K. Yonekura, C. Toyoshima, S. Maki-Yonekura, and K. Namba: GUI programs for processing individual images in early stages of helical image reconstruction-for high-resolution structure analysis. J. Struct. Biol. 144 (2003) 184-194. [pubmed]
45. C. Toyoshima, H. Nomura and Y. Sugita: Structural basis of ion pumping by Ca²⁺-ATPase of sarcoplasmic reticulum. FEBS Letters 555 (2003) 106-110. [pubmed]
46. H. Ma, G. Inesi and C. Toyoshima: Substrate-induced conformational fit and headpiece closure in the Ca²⁺ATPase (SERCA). J. Biol. Chem. 278 (2003) 28938-28943. [pubmed]
47. M. Asahi, Y. Sugita, K. Kurzydlowski, S. De Leon, M. Tada, C. Toyoshima and D.H. MacLennan: Sarcolipin regulates sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban. Proc. Nat. Acad. Sci. USA. 100 (2003) 5040-5045. [pubmed]
48. C. Toyoshima, M. Asahi, Y. Sugita, R. Khanna, T. Tsuda and D.H. MacLennan: Modeling of the inhibitory interaction of phospholamban with the Ca²⁺ATPase. Proc. Nat. Acad. Sci. USA. 100 (2003) 467-472. [pubmed]
49. C. Toyoshima and H. Nomura: Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418 (2002) 605-611. [pubmed] [reprint] [Supplement]
50. H. Ogawa and C. Toyoshima: Homology modeling of the cation binding sites of Na+K+-ATPase. Proc. Nat. Acad. Sci. USA. 99 (2002) 15977-15982. [pubmed]
51. S. Hua, H. Ma, D. Lewis, G. Inesi and C. Toyoshima: Functional role of “N” (Nucleotide) and “P” (Phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase. Biochemistry 41(2002) 2264-2272. [pubmed]
52. S. Hua, G. Inesi, H. Nomura and C. Toyoshima: Fe²⁺-catalyzed oxidation and cleavage of sarcoplasmic reticulum ATPase reveals Mg²⁺ and Mg²⁺-ATP sites. Biochemistry 41 (2002) 11405-11410. [pubmed]
53. J. V. Moller, G. Lenoir, C. Marchand, C. Montigny, M. le Maire, C. Toyoshima, B. S. Juul and P. Champeil: Calcium transport by sarcoplasmic reticulum Ca²⁺-ATPase: role of the A-domain and its C-terminal link with the transmembrane region. J. Biol. Chem. 277 (2002) 38647-38659. [pubmed]
54. S. Danko, K. Yamasaki, T. Daiho, H. Suzuki, C. Toyoshima: Organization of cytoplasmic domains of sarcoplasmic reticulum Ca²⁺-ATPase in E1P and E1ATP states: a limited proteolysis study. FEBS letters 505 (2001) 129-135. [pubmed]
55. S. Danko, T. Daiho, K. Yamasaki, M. Kamidochi, H. Suzuki, C. Toyoshima: ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca²⁺-ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin. FEBS letters 489 (2001) 277-282. [pubmed]
56. Z. Zhang, D. Lewis, C. Sumbilla, G. Inesi, and C. Toyoshima: The role of the M6-M7 Loop (L67) in stabilization of the phosphorylation and Ca²⁺ binding domains of the sarcoplasmic reticulum Ca²⁺-ATPase (SERCA). J. Biol. Chem. 276 (2001) 15232-15239. [pubmed]
57. C. Toyoshima, M. Nakasako, H. Nomura and H. Ogawa: Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405 (2000) 647-655. [pubmed] [reprint]
58. C. Toyoshima: Structure determination of tubular crystals of membrane proteins. I. Indexing of diffraction patterns. Ultramicroscopy 84 (2000) 1-14. [pubmed]
59. K. Yonekura and C. Toyoshima: Structure determination of tubular crystals of membrane proteins. II. Averaging of tubular crystals of different helical classes. Ultramicroscopy 84 (2000) 15-28. [pubmed]
60. K. Yonekura and C. Toyoshima: Structure determination of tubular crystals of membrane proteins. III. Solvent flattening. Ultramicroscopy 84 (2000) 29-45. [pubmed]
61. H. Ogawa, T. Haga and C. Toyoshima: Soluble P-type ATPase from an archaeon, Methanococcus jannaschii. FEBS letters 471 (2000) 99-102. [pubmed]
62. S. Hua, G. Inesi and C. Toyoshima: Distinct topologies of mono-and decavanadate binding and photo-oxidative cleavage in the sarcoplasmic reticulum ATPase. J. Biol. Chem. 275 (2000) 30546-30550. [pubmed]
63. Z. Zhang, D. Lewis, C. Strock, G. Inesi, M. Nakasako, H. Nomura and C. Toyoshima: Detailed characterization of the cooperative mechanism of Ca²⁺ binding and catalytic activation in the Ca²⁺ transport (SERCA) ATPase. Biochemistry 39 (2000) 8758-8767. [pubmed]
64. K. Hirose, U. Henningsen, M. Schliwa, C. Toyoshima, T. Shimizu and M. Alonso, R.A.Cross and L.A. Amos: Structural comparison of dimeric Eg5, Neurospora Kinesin (Nkin) and Ncd Head-Nkin Neck chimera with conventional Kinesin. EMBO Journal, 19 (2000) 5308-5314. [pubmed]
65. K. Mayanagi, T. Ishikawa, C. Toyoshima, Y. Inoue and K. Nakazato: Three-dimensional electron microscopy of the photosystem II core complex. J. Struct. Biol. 123 (1998) 211-224 [pubmed].
66. H. Ogawa, D.L. Stokes, H. Sasabe and C. Toyoshima: Structure of the Ca²⁺ pump of sarcoplasmic reticulum: A view along the lipid bilayer at 9-A resolution. Biophys. J. 75 (1998) 41-52. [pubmed]
67. P. Zhang, C. Toyoshima, K. Yonekura, N.M. Green and D.L. Stokes: Structure of the calcium pump from sarcoplasmic reticulum at 8 A resolution. Nature 392 (1998) 835-839. [pubmed] [reprint]
68. K. Yonekura, D.L. Stokes, H. Sasabe and C. Toyoshima: The ATP binding site of Ca²⁺-ATPase revealed by electron image analysis. Biophys. J. 72 (1997) 997-1005. [pubmed]
69. K. Tani, H. Sasabe and C. Toyoshima: A set of computer programs for determining defocus and astigmatism in electron images. Ultramicroscopy 65 (1996) 31-44.
70. T. Akiba, C. Toyoshima, T. Matsunaga, M. Kawamoto, T. Kubota, K. Fukuyama, K. Namba and H. Matsubara: Three-dimensional structure of bovine cytochrome bc1 complex by electron cryomicroscopy and helical image reconstruction. Nature Struct. Biol. 3 (1996) 553-561. [pubmed]
71. G-W. Choeng, H.S. Young, H. Ogawa, C. Toyoshima D.L. Stokes: Lamellar stacking in three-dimensional crystals of Ca²⁺-ATPase from sarcoplasmic reticulum. Biophys. J. 70 (1996) 1689-1699. [pubmed]
72. K. Nakazato, C. Toyoshima, I. Enami and Y. Inoue: Two-dimensional Crystallization and cryo-electron microscopy of photosystem II. J. Mol. Biol. 257 (1996) 225-232. [pubmed]
73. M. Nakasako, T. Ueki, C. Toyoshima and Y. Umeda: A crystal mounting device made from a capillary tube for cryogenic macromolecular crystallography. J. Appl. Cryst. 28 (1995) 856-857.
74. Y. Mimori, I. Yamashita, K. Murata, Y. Fujiyoshi, K. Yonekura, C. Toyoshima and K. Namba: The Structure of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy. J. Mol. Biol. 249 (1995) 69-87. [pubmed]
75. C. Toyoshima, H. Sasabe and D.L. Stokes: Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 362 (1993) 469-471. [pubmed]
76. C. Toyoshima, K. Yonekura and H. Sasabe: Contrast transfer for the frozen hydrated specimen. II: Amplitude contrast at very low frequencies. Ultramicroscopy 48 (1993) 165-176.
77. A. Sato, T. Furuno, C. Toyoshima and H. Sasabe: Two-dimensional crystallization of catalase on a monolayer film of poly (1-benzyl-L-histidine) spread at the air/water interface. Biochim. Biophys. Acta 1162 (1993) 54-60. [pubmed]
78. K. Yamane, C. Toyoshima and S. Nishimura: Ligand-induced functions of the epidermal growth factor receptor require the positively charged region asymmetrically distributed across plasma membrane. Biochem. Biophys. Res. Comm. 184 (1992) 1301-1310. [pubmed]
79. C. Toyoshima and N. Unwin: Three-dimensional structure of the acetylcholine receptor by cryo-electron microscopy and helical reconstruction. J. Cell. Biol. 111 (1990) 2623-2635. [pubmed]
80. C. Toyoshima: On the use of holey grids in electron crystallography. Ultramicroscopy 30 (1989) 439-444.
81. Y.Y. Toyoshima, C. Toyoshima and J.A. Spudich: Bidirectional movement of actin filaments along tracks of myosin heads. Nature 341 (1989) 154-156. [pubmed]
82. T. Miyanishi, C. Toyoshima, T. Wakabayashi and G. Matsuda: Electron microscopic study on the location of 23K and 50K fragments in skeletal myosin head. J. Biochem. 103 (1988) 458-462. [pubmed]
83. C. Toyoshima and N. Unwin: Contrast transfer for the frozen hydrated specimen: determination from pairs of defocused images. Ultramicroscopy 25 (1988) 279-292. [pubmed]
84. N. Unwin, C. Toyoshima and E. Kubalek: Arrangement of the acetylcholine receptor subunits in the resting and desensitized states, determined by cryo-electron microscopy of crystallized Torpedo postsynaptic membranes. J. Cell. Biol.107 (1988) 1123-1138. [pubmed]
85. C. Toyoshima and N. Unwin: Ion channel of the acetylcholine receptor reconstructed from images of postsynaptic membranes. Nature 336 (1988) 247-250. [pubmed]
86. Y.Y. Toyoshima, S.J. Kron, E.M. McNally, K.R. Niebling, C. Toyoshima and J.A. Spudich: Myosin Subfrgment-1 is sufficient to move actin filaments in vitro. Nature 328 (1987) 536-539. [pubmed]
87. M. Tokunaga, K. Sutoh, C. Toyoshima and T. Wakabayashi: Location of the ATPase site of myosin determined by three-dimensional electron microscopy. Nature 329 (1987) 635-638. [pubmed]
88. C. Toyoshima and T. Wakabayashi: Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. IV. Reconstitution from minimal- and high-dose images of Actin-tropomyosin-myosin Subfragment-1 Complex. J. Biochem., 97 (1985) 219-243. [pubmed]
89. C. Toyoshima and T. Wakabayashi: Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. assignment of actin in the actin-tropomyosin-myosin Subfragment-1 complex. J. Biochem., 97 (1985) 245-263. [pubmed]
90. Y. Yano, T. Mohri, C. Toyoshima and T. Wakabayashi: Molecular structure of dynein arms. J. Submicroscopic Cytol., 15 (1983) 211-215.
91. T. Wakabayashi and C. Toyoshima: Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. II. The multi-domain structure of Actin-myosin S1 complex. J. Biochem., 90 (1981) 683-701. [pubmed]
92. C. Toyoshima and T. Wakabayashi: Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. I. Tilt angle of myosin Subfragment-1 in rigor complex. J. Biochem., 86, (1979) 1887-1890. [pubmed]