In vivo protein crystallization opens new routes in structural biology

Rudolf Koopmann; Karolina Cupelli; Lars Redecke; Karol Nass; Daniel P. Deponte; Thomas A. White; Francesco Stellato; Dirk Rehders; Mengning Liang; Jakob Andreasson; Andrew Aquila; Sasa Bajt; Miriam Barthelmess; Anton Barty; Michael J. Bogan; Christoph Bostedt; Sébastien Boutet; John D. Bozek; Carl Caleman; Nicola Coppola; Jan Davidsson; R. Bruce Doak; Tomas Ekeberg; Sascha W. Epp; Benjamin Erk; Holger Fleckenstein; Lutz Foucar; Heinz Graafsma; Lars Gumprecht; Janos Hajdu; Christina Y. Hampton; Andreas Hartmann; Robert Hartmann; Gülnter Hauser; Helmut Hirsemann; Peter Holl; Mark S. Hunter; Stephan Kassemeyer; Richard Kirian; Lukas Lomb; Filipe R N C Maia; Nils Kimmel; Andrew V. Martin; Marc Messerschmidt; Christian Reich; Daniel Rolles; Benedikt Rudek; Artem Rudenko; Ilme Schlichting; Joachim Schulz; M. Marvin Seibert; Robert L. Shoeman; Raymond G. Sierra; Heike Soltau; Stephan Stern; Lothar Strülder; Nicusor Timneanu; Joachim Ullrich; Xiaoyu Wang; Georg Weidenspointner; Uwe Weierstall; Garth J. Williams; Cornelia B. Wunderer; Petra Fromme; John Spence; Thilo Stehle; Henry N. Chapman; Christian Betzel; Michael Duszenko

doi:10.1038/nmeth.1859

In vivo protein crystallization opens new routes in structural biology

Rudolf Koopmann, Karolina Cupelli, Lars Redecke, Karol Nass, Daniel P. Deponte, Thomas A. White, Francesco Stellato, Dirk Rehders, Mengning Liang, Jakob Andreasson, Andrew Aquila, Sasa Bajt, Miriam Barthelmess, Anton Barty, Michael J. Bogan, Christoph Bostedt, Sébastien Boutet, John D. Bozek, Carl Caleman, Nicola CoppolaJan Davidsson, R. Bruce Doak, Tomas Ekeberg, Sascha W. Epp, Benjamin Erk, Holger Fleckenstein, Lutz Foucar, Heinz Graafsma, Lars Gumprecht, Janos Hajdu, Christina Y. Hampton, Andreas Hartmann, Robert Hartmann, Gülnter Hauser, Helmut Hirsemann, Peter Holl, Mark S. Hunter, Stephan Kassemeyer, Richard Kirian, Lukas Lomb, Filipe R N C Maia, Nils Kimmel, Andrew V. Martin, Marc Messerschmidt, Christian Reich, Daniel Rolles, Benedikt Rudek, Artem Rudenko, Ilme Schlichting, Joachim Schulz, M. Marvin Seibert, Robert L. Shoeman, Raymond G. Sierra, Heike Soltau, Stephan Stern, Lothar Strülder, Nicusor Timneanu, Joachim Ullrich, Xiaoyu Wang, Georg Weidenspointner, Uwe Weierstall, Garth J. Williams, Cornelia B. Wunderer, Petra Fromme, John Spence, Thilo Stehle, Henry N. Chapman, Christian Betzel, Michael Duszenko

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Abstract

Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis. We prepared nano-sized in vivo-grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free-electron laser-based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology.

Original language	English (US)
Pages (from-to)	259-262
Number of pages	4
Journal	Nature Methods
Volume	9
Issue number	3
DOIs	https://doi.org/10.1038/nmeth.1859
State	Published - Mar 2012

ASJC Scopus subject areas

Biotechnology
Biochemistry
Molecular Biology
Cell Biology

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Koopmann, R., Cupelli, K., Redecke, L., Nass, K., Deponte, D. P., White, T. A., Stellato, F., Rehders, D., Liang, M., Andreasson, J., Aquila, A., Bajt, S., Barthelmess, M., Barty, A., Bogan, M. J., Bostedt, C., Boutet, S., Bozek, J. D., Caleman, C., ... Duszenko, M. (2012). In vivo protein crystallization opens new routes in structural biology. Nature Methods, 9(3), 259-262. https://doi.org/10.1038/nmeth.1859

Koopmann, R, Cupelli, K, Redecke, L, Nass, K, Deponte, DP, White, TA, Stellato, F, Rehders, D, Liang, M, Andreasson, J, Aquila, A, Bajt, S, Barthelmess, M, Barty, A, Bogan, MJ, Bostedt, C, Boutet, S, Bozek, JD, Caleman, C, Coppola, N, Davidsson, J, Doak, RB, Ekeberg, T, Epp, SW, Erk, B, Fleckenstein, H, Foucar, L, Graafsma, H, Gumprecht, L, Hajdu, J, Hampton, CY, Hartmann, A, Hartmann, R, Hauser, G, Hirsemann, H, Holl, P, Hunter, MS, Kassemeyer, S, Kirian, R, Lomb, L, Maia, FRNC, Kimmel, N, Martin, AV, Messerschmidt, M, Reich, C, Rolles, D, Rudek, B, Rudenko, A, Schlichting, I, Schulz, J, Seibert, MM, Shoeman, RL, Sierra, RG, Soltau, H, Stern, S, Strülder, L, Timneanu, N, Ullrich, J, Wang, X, Weidenspointner, G, Weierstall, U, Williams, GJ, Wunderer, CB, Fromme, P, Spence, J, Stehle, T, Chapman, HN, Betzel, C & Duszenko, M 2012, 'In vivo protein crystallization opens new routes in structural biology', Nature Methods, vol. 9, no. 3, pp. 259-262. https://doi.org/10.1038/nmeth.1859

@article{0f1b6a379e8d447489195d0747bb91a4,

title = "In vivo protein crystallization opens new routes in structural biology",

abstract = "Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis. We prepared nano-sized in vivo-grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free-electron laser-based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology.",

author = "Rudolf Koopmann and Karolina Cupelli and Lars Redecke and Karol Nass and Deponte, {Daniel P.} and White, {Thomas A.} and Francesco Stellato and Dirk Rehders and Mengning Liang and Jakob Andreasson and Andrew Aquila and Sasa Bajt and Miriam Barthelmess and Anton Barty and Bogan, {Michael J.} and Christoph Bostedt and S{\'e}bastien Boutet and Bozek, {John D.} and Carl Caleman and Nicola Coppola and Jan Davidsson and Doak, {R. Bruce} and Tomas Ekeberg and Epp, {Sascha W.} and Benjamin Erk and Holger Fleckenstein and Lutz Foucar and Heinz Graafsma and Lars Gumprecht and Janos Hajdu and Hampton, {Christina Y.} and Andreas Hartmann and Robert Hartmann and G{\"u}lnter Hauser and Helmut Hirsemann and Peter Holl and Hunter, {Mark S.} and Stephan Kassemeyer and Richard Kirian and Lukas Lomb and Maia, {Filipe R N C} and Nils Kimmel and Martin, {Andrew V.} and Marc Messerschmidt and Christian Reich and Daniel Rolles and Benedikt Rudek and Artem Rudenko and Ilme Schlichting and Joachim Schulz and Seibert, {M. Marvin} and Shoeman, {Robert L.} and Sierra, {Raymond G.} and Heike Soltau and Stephan Stern and Lothar Str{\"u}lder and Nicusor Timneanu and Joachim Ullrich and Xiaoyu Wang and Georg Weidenspointner and Uwe Weierstall and Williams, {Garth J.} and Wunderer, {Cornelia B.} and Petra Fromme and John Spence and Thilo Stehle and Chapman, {Henry N.} and Christian Betzel and Michael Duszenko",

note = "Funding Information: FEL experiments were carried out at LCLS in June 2010 (TbCatB) and in August 2011 (TbIMPDH), a national user facility operated by Stanford University on behalf of the US Department of Energy, Office of Basic Energy Sciences. The X-ray diffraction experiments on recrystallized TbCatB crystals were carried out at beamline X06DA of the Swiss Light Source (Villigen, Switzerland). This work was supported in part by a grant from the Deutsche Forschungsgemeinschaft (DFG), from the Swedish Research Council, from the Knut och Alice Wallenbergs Stiftelse, from the European Research Council, as well as by US National Science Foundation award MCB-1021557. R.K. received a fellowship from the Landesgraduiertenf{\"o}rderung Baden-W{\"u}rttemberg. L.R., D. Rehders and C. Betzel thank the German Federal Ministry for Education and Research for funding (grants 01KX0806 and 01KX0807). Support from the Hamburg Ministry of Science and Research and Joachim Herz Stiftung as part of the Hamburg Initiative for Excellence in Research and the Hamburg School for Structure and Dynamics in infection, and from the DFG Cluster of Excellence “Inflammation at Interfaces” (EXC 306) is gratefully acknowledged. Funding Information: Funding for the development and operation of the CFEL-ASG multipurpose (CAMP) instrument within the Advanced Study Group at the Center for Free-Electron Laser Science was provided by the Max Planck Society. M.J.B., R.G.S. and C.Y.H. acknowledge funding from the US Department of Energy Office of Basic Energy Sciences through the Photon Ultrafast Laser Science and Engineering (PULSE) Institute at the Stanford Linear Accelerator Center (SLAC) National Accelerator Laboratory.",

year = "2012",

month = mar,

doi = "10.1038/nmeth.1859",

language = "English (US)",

volume = "9",

pages = "259--262",

journal = "Nature Methods",

issn = "1548-7091",

publisher = "Nature Publishing Group",

number = "3",

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TY - JOUR

T1 - In vivo protein crystallization opens new routes in structural biology

AU - Koopmann, Rudolf

AU - Cupelli, Karolina

AU - Redecke, Lars

AU - Nass, Karol

AU - Deponte, Daniel P.

AU - White, Thomas A.

AU - Stellato, Francesco

AU - Rehders, Dirk

AU - Liang, Mengning

AU - Andreasson, Jakob

AU - Aquila, Andrew

AU - Bajt, Sasa

AU - Barthelmess, Miriam

AU - Barty, Anton

AU - Bogan, Michael J.

AU - Bostedt, Christoph

AU - Boutet, Sébastien

AU - Bozek, John D.

AU - Caleman, Carl

AU - Coppola, Nicola

AU - Davidsson, Jan

AU - Doak, R. Bruce

AU - Ekeberg, Tomas

AU - Epp, Sascha W.

AU - Erk, Benjamin

AU - Fleckenstein, Holger

AU - Foucar, Lutz

AU - Graafsma, Heinz

AU - Gumprecht, Lars

AU - Hajdu, Janos

AU - Hampton, Christina Y.

AU - Hartmann, Andreas

AU - Hartmann, Robert

AU - Hauser, Gülnter

AU - Hirsemann, Helmut

AU - Holl, Peter

AU - Hunter, Mark S.

AU - Kassemeyer, Stephan

AU - Kirian, Richard

AU - Lomb, Lukas

AU - Maia, Filipe R N C

AU - Kimmel, Nils

AU - Martin, Andrew V.

AU - Messerschmidt, Marc

AU - Reich, Christian

AU - Rolles, Daniel

AU - Rudek, Benedikt

AU - Rudenko, Artem

AU - Schlichting, Ilme

AU - Schulz, Joachim

AU - Seibert, M. Marvin

AU - Shoeman, Robert L.

AU - Sierra, Raymond G.

AU - Soltau, Heike

AU - Stern, Stephan

AU - Strülder, Lothar

AU - Timneanu, Nicusor

AU - Ullrich, Joachim

AU - Wang, Xiaoyu

AU - Weidenspointner, Georg

AU - Weierstall, Uwe

AU - Williams, Garth J.

AU - Wunderer, Cornelia B.

AU - Fromme, Petra

AU - Spence, John

AU - Stehle, Thilo

AU - Chapman, Henry N.

AU - Betzel, Christian

AU - Duszenko, Michael

N1 - Funding Information: FEL experiments were carried out at LCLS in June 2010 (TbCatB) and in August 2011 (TbIMPDH), a national user facility operated by Stanford University on behalf of the US Department of Energy, Office of Basic Energy Sciences. The X-ray diffraction experiments on recrystallized TbCatB crystals were carried out at beamline X06DA of the Swiss Light Source (Villigen, Switzerland). This work was supported in part by a grant from the Deutsche Forschungsgemeinschaft (DFG), from the Swedish Research Council, from the Knut och Alice Wallenbergs Stiftelse, from the European Research Council, as well as by US National Science Foundation award MCB-1021557. R.K. received a fellowship from the Landesgraduiertenförderung Baden-Württemberg. L.R., D. Rehders and C. Betzel thank the German Federal Ministry for Education and Research for funding (grants 01KX0806 and 01KX0807). Support from the Hamburg Ministry of Science and Research and Joachim Herz Stiftung as part of the Hamburg Initiative for Excellence in Research and the Hamburg School for Structure and Dynamics in infection, and from the DFG Cluster of Excellence “Inflammation at Interfaces” (EXC 306) is gratefully acknowledged. Funding Information: Funding for the development and operation of the CFEL-ASG multipurpose (CAMP) instrument within the Advanced Study Group at the Center for Free-Electron Laser Science was provided by the Max Planck Society. M.J.B., R.G.S. and C.Y.H. acknowledge funding from the US Department of Energy Office of Basic Energy Sciences through the Photon Ultrafast Laser Science and Engineering (PULSE) Institute at the Stanford Linear Accelerator Center (SLAC) National Accelerator Laboratory.

PY - 2012/3

Y1 - 2012/3

N2 - Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis. We prepared nano-sized in vivo-grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free-electron laser-based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology.

AB - Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis. We prepared nano-sized in vivo-grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free-electron laser-based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology.

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SP - 259

EP - 262

JO - Nature Methods

JF - Nature Methods

IS - 3

ER -

In vivo protein crystallization opens new routes in structural biology

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