Reich C, Pietschner D, Struder L, Hauser G, Gorke H, Ullrich J, Herrmann S, Schaller G,
Schopper F, Soltau H, Kuhnel KU, Messerschmidt M, Bozek JD, Hau-Riege SP, Frank M,
Hampton CY, Sierra RG, Starodub D, Williams GJ, Hajdu J, Timneanu N, Seibert MM,
Andreasson J, Rocker A, Jonsson O, Svenda M, Stern S, Nass K, Andritschke R, Schroter CD,
Krasniqi F, Bott M, Schmidt KE, Wang XY, Grotjohann I, Holton JM, Barends TRM,
Neutze R, Marchesini S, Fromme R, Schorb S, Rupp D, Adolph M, Gorkhover T,
Andersson I, Hirsemann H, Potdevin G, Graafsma H, Nilsson B, Spence JCH (2011) Femtosecond X-ray protein nanocrystallography. Nature 470(7332):73–U81
46. Schmidt M, Pande K, Basu S, Tenboer J (2015) Room temperature structures beyond 1.5
angstrom by serial femtosecond crystallography. Struct Dyn 2(4)
47. Coppens P, Fournier B (2015) On the scaling of multicrystal data sets collected at highintensity X-ray and electron sources. Struct Dyn 2(6)
48. Srajer V, Teng TY, Ursby T, Pradervand C, Ren Z, Adachi S, Schildkamp W, Bourgeois D,
Wulff M, Moffat K (1996) Photolysis of the carbon monoxide complex of myoglobin:
nanosecond time-resolved crystallography. Science 274(5293):1726–1729
49. Lim MH, Jackson TA, Anfinrud PA (1995) Midinfrared vibrational-spectrum of co after
photodissociation from heme evidence for a ligand docking site in the heme pocket of
hemoglobin and myoglobin. J Chem Phys 102(11):4355–4366
50. Lim M, Jackson TA, Anfinrud PA (1995) Binding of co to myoglobin from a heme pocket
docking site to form nearly linear FE-C-O. Science 269(5226):962–966
51. Franzen S, Bohn B, Poyart C, Martin JL (1995) Evidence for subpicosecond heme doming in
hemoglobin and myoglobin – a time-resolved resonance Raman comparison of carbonmonoxy
and deoxy species. Biochemistry 34(4):1224–1237
52. Srajer V, Ren Z, Teng TY, Schmidt M, Ursby T, Bourgeois D, Pradervand C, Schildkamp W,
Wulff M, Moffat K (2001) Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction. Biochemistry 40(46):13802–13815
53. Jung YO, Lee JH, Kim J, Schmidt M, Moffat K, Šrajer V, Ihee H (2013) Volume-conserving
trans–cis isomerization pathways in photoactive yellow protein visualized by picosecond
X-ray crystallography. Nat Chem 5(3):212–220
54. Schotte F, Cho HS, Kaila VRI, Kamikubo H, Dashdorj N, Henry ER, Graber TJ, Henning R,
Wulff M, Hummer G, Kataoka M, Anfinrud PA (2012) Watching a signaling protein function
in real time via 100-ps time-resolved Laue crystallography. Proc Natl Acad Sci 109
(47):19256–19261
55. Ren Z, Perman B, Šrajer V, Teng TY, Pradervand C, Bourgeois D, Schotte F, Ursby T, Kort R,
Wulff M, Moffat K (2001) A molecular movie at 1.8 Å resolution displays the photocycle of
photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds.
Biochemistry 40(46):13788–13801
56. Helliwell JR, Mitchell EP (2015) Synchrotron radiation macromolecular crystallography:
science and spin-offs. Iucrj 2:283–291
57. Moffat K (2014) Time-resolved crystallography and protein design: signalling photoreceptors
and optogenetics. Philos Trans R Soc B Biol Sci 369(1647):20130568
58. Moffat K (2001) Time-resolved biochemical crystallography: a mechanistic perspective.
Chem Rev 101(6):1569–1581
59. Schmidt M (2019) Time-resolved macromolecular crystallography at pulsed X-ray sources. Int
J Mol Sci 20(6)
60. Nam KH (2019) Sample delivery Media for Serial Crystallography. Int J Mol Sci 20(5)
61. Chapman HN (2019) X-ray free-electron lasers for the structure and dynamics of macromolecules. In: Kornberg RD (ed) Annual review of biochemistry, vol 88. Annual Reviews,
pp 35–58
62. Srajer V, Schmidt M (2017) Watching proteins function with time-resolved x-ray crystallography. J Phys D Appl Phys 50(37)
63. Johansson LC, Stauch B, Ishchenko A, Cherezov V (2017) A bright future for serial femtosecond crystallography with XFELs. Trends Biochem Sci 42(9):749–762
Time-Resolved Single-Crystal X-Ray Crystallography
267
Schopper F, Soltau H, Kuhnel KU, Messerschmidt M, Bozek JD, Hau-Riege SP, Frank M,
Hampton CY, Sierra RG, Starodub D, Williams GJ, Hajdu J, Timneanu N, Seibert MM,
Andreasson J, Rocker A, Jonsson O, Svenda M, Stern S, Nass K, Andritschke R, Schroter CD,
Krasniqi F, Bott M, Schmidt KE, Wang XY, Grotjohann I, Holton JM, Barends TRM,
Neutze R, Marchesini S, Fromme R, Schorb S, Rupp D, Adolph M, Gorkhover T,
Andersson I, Hirsemann H, Potdevin G, Graafsma H, Nilsson B, Spence JCH (2011) Femtosecond X-ray protein nanocrystallography. Nature 470(7332):73–U81
46. Schmidt M, Pande K, Basu S, Tenboer J (2015) Room temperature structures beyond 1.5
angstrom by serial femtosecond crystallography. Struct Dyn 2(4)
47. Coppens P, Fournier B (2015) On the scaling of multicrystal data sets collected at highintensity X-ray and electron sources. Struct Dyn 2(6)
48. Srajer V, Teng TY, Ursby T, Pradervand C, Ren Z, Adachi S, Schildkamp W, Bourgeois D,
Wulff M, Moffat K (1996) Photolysis of the carbon monoxide complex of myoglobin:
nanosecond time-resolved crystallography. Science 274(5293):1726–1729
49. Lim MH, Jackson TA, Anfinrud PA (1995) Midinfrared vibrational-spectrum of co after
photodissociation from heme evidence for a ligand docking site in the heme pocket of
hemoglobin and myoglobin. J Chem Phys 102(11):4355–4366
50. Lim M, Jackson TA, Anfinrud PA (1995) Binding of co to myoglobin from a heme pocket
docking site to form nearly linear FE-C-O. Science 269(5226):962–966
51. Franzen S, Bohn B, Poyart C, Martin JL (1995) Evidence for subpicosecond heme doming in
hemoglobin and myoglobin – a time-resolved resonance Raman comparison of carbonmonoxy
and deoxy species. Biochemistry 34(4):1224–1237
52. Srajer V, Ren Z, Teng TY, Schmidt M, Ursby T, Bourgeois D, Pradervand C, Schildkamp W,
Wulff M, Moffat K (2001) Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction. Biochemistry 40(46):13802–13815
53. Jung YO, Lee JH, Kim J, Schmidt M, Moffat K, Šrajer V, Ihee H (2013) Volume-conserving
trans–cis isomerization pathways in photoactive yellow protein visualized by picosecond
X-ray crystallography. Nat Chem 5(3):212–220
54. Schotte F, Cho HS, Kaila VRI, Kamikubo H, Dashdorj N, Henry ER, Graber TJ, Henning R,
Wulff M, Hummer G, Kataoka M, Anfinrud PA (2012) Watching a signaling protein function
in real time via 100-ps time-resolved Laue crystallography. Proc Natl Acad Sci 109
(47):19256–19261
55. Ren Z, Perman B, Šrajer V, Teng TY, Pradervand C, Bourgeois D, Schotte F, Ursby T, Kort R,
Wulff M, Moffat K (2001) A molecular movie at 1.8 Å resolution displays the photocycle of
photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds.
Biochemistry 40(46):13788–13801
56. Helliwell JR, Mitchell EP (2015) Synchrotron radiation macromolecular crystallography:
science and spin-offs. Iucrj 2:283–291
57. Moffat K (2014) Time-resolved crystallography and protein design: signalling photoreceptors
and optogenetics. Philos Trans R Soc B Biol Sci 369(1647):20130568
58. Moffat K (2001) Time-resolved biochemical crystallography: a mechanistic perspective.
Chem Rev 101(6):1569–1581
59. Schmidt M (2019) Time-resolved macromolecular crystallography at pulsed X-ray sources. Int
J Mol Sci 20(6)
60. Nam KH (2019) Sample delivery Media for Serial Crystallography. Int J Mol Sci 20(5)
61. Chapman HN (2019) X-ray free-electron lasers for the structure and dynamics of macromolecules. In: Kornberg RD (ed) Annual review of biochemistry, vol 88. Annual Reviews,
pp 35–58
62. Srajer V, Schmidt M (2017) Watching proteins function with time-resolved x-ray crystallography. J Phys D Appl Phys 50(37)
63. Johansson LC, Stauch B, Ishchenko A, Cherezov V (2017) A bright future for serial femtosecond crystallography with XFELs. Trends Biochem Sci 42(9):749–762
Time-Resolved Single-Crystal X-Ray Crystallography
267