In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?

Francois-Xavier Gallat, Naohiro Matsugaki, Nathan P Coussens, Koichiro J Yagi, Marion Boudes, Tetsuya Higashi, Daisuke Tsuji, Yutaka Tatano, Mamoru Suzuki, Eiichi Mizohata, Kensuke Tono, Yasumasa Joti, Takashi Kameshima, Jaehyun Park, Changyong Song, Takaki Hatsui, Makina Yabashi, Eriko Nango, Kohji Itoh, Fasseli J Coulibaly & 5 others Stephen S Tobe, Subramanian Ramaswamy, Barbara Stay, So Iwata, Leonard M G Chavas

Research output: Contribution to journalArticleResearchpeer-review

Abstract

The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography.
Original languageEnglish
Pages (from-to)1 - 4
Number of pages4
JournalPhilosophical Transactions of the Royal Society B: Biological Sciences
Volume369
Issue number1647 (Art. No: 20130497)
DOIs
Publication statusPublished - 2014

Cite this

Gallat, Francois-Xavier ; Matsugaki, Naohiro ; Coussens, Nathan P ; Yagi, Koichiro J ; Boudes, Marion ; Higashi, Tetsuya ; Tsuji, Daisuke ; Tatano, Yutaka ; Suzuki, Mamoru ; Mizohata, Eiichi ; Tono, Kensuke ; Joti, Yasumasa ; Kameshima, Takashi ; Park, Jaehyun ; Song, Changyong ; Hatsui, Takaki ; Yabashi, Makina ; Nango, Eriko ; Itoh, Kohji ; Coulibaly, Fasseli J ; Tobe, Stephen S ; Ramaswamy, Subramanian ; Stay, Barbara ; Iwata, So ; Chavas, Leonard M G. / In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?. In: Philosophical Transactions of the Royal Society B: Biological Sciences. 2014 ; Vol. 369, No. 1647 (Art. No: 20130497). pp. 1 - 4.
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title = "In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?",
abstract = "The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography.",
author = "Francois-Xavier Gallat and Naohiro Matsugaki and Coussens, {Nathan P} and Yagi, {Koichiro J} and Marion Boudes and Tetsuya Higashi and Daisuke Tsuji and Yutaka Tatano and Mamoru Suzuki and Eiichi Mizohata and Kensuke Tono and Yasumasa Joti and Takashi Kameshima and Jaehyun Park and Changyong Song and Takaki Hatsui and Makina Yabashi and Eriko Nango and Kohji Itoh and Coulibaly, {Fasseli J} and Tobe, {Stephen S} and Subramanian Ramaswamy and Barbara Stay and So Iwata and Chavas, {Leonard M G}",
year = "2014",
doi = "10.1098/rstb.2013.0497",
language = "English",
volume = "369",
pages = "1 -- 4",
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Gallat, F-X, Matsugaki, N, Coussens, NP, Yagi, KJ, Boudes, M, Higashi, T, Tsuji, D, Tatano, Y, Suzuki, M, Mizohata, E, Tono, K, Joti, Y, Kameshima, T, Park, J, Song, C, Hatsui, T, Yabashi, M, Nango, E, Itoh, K, Coulibaly, FJ, Tobe, SS, Ramaswamy, S, Stay, B, Iwata, S & Chavas, LMG 2014, 'In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?' Philosophical Transactions of the Royal Society B: Biological Sciences, vol. 369, no. 1647 (Art. No: 20130497), pp. 1 - 4. https://doi.org/10.1098/rstb.2013.0497

In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology? / Gallat, Francois-Xavier; Matsugaki, Naohiro; Coussens, Nathan P; Yagi, Koichiro J; Boudes, Marion; Higashi, Tetsuya; Tsuji, Daisuke; Tatano, Yutaka; Suzuki, Mamoru; Mizohata, Eiichi; Tono, Kensuke; Joti, Yasumasa; Kameshima, Takashi; Park, Jaehyun; Song, Changyong; Hatsui, Takaki; Yabashi, Makina; Nango, Eriko; Itoh, Kohji; Coulibaly, Fasseli J; Tobe, Stephen S; Ramaswamy, Subramanian; Stay, Barbara; Iwata, So; Chavas, Leonard M G.

In: Philosophical Transactions of the Royal Society B: Biological Sciences, Vol. 369, No. 1647 (Art. No: 20130497), 2014, p. 1 - 4.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology?

AU - Gallat, Francois-Xavier

AU - Matsugaki, Naohiro

AU - Coussens, Nathan P

AU - Yagi, Koichiro J

AU - Boudes, Marion

AU - Higashi, Tetsuya

AU - Tsuji, Daisuke

AU - Tatano, Yutaka

AU - Suzuki, Mamoru

AU - Mizohata, Eiichi

AU - Tono, Kensuke

AU - Joti, Yasumasa

AU - Kameshima, Takashi

AU - Park, Jaehyun

AU - Song, Changyong

AU - Hatsui, Takaki

AU - Yabashi, Makina

AU - Nango, Eriko

AU - Itoh, Kohji

AU - Coulibaly, Fasseli J

AU - Tobe, Stephen S

AU - Ramaswamy, Subramanian

AU - Stay, Barbara

AU - Iwata, So

AU - Chavas, Leonard M G

PY - 2014

Y1 - 2014

N2 - The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography.

AB - The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography.

UR - http://rstb.royalsocietypublishing.org/content/369/1647/20130497.full-text.pdf

U2 - 10.1098/rstb.2013.0497

DO - 10.1098/rstb.2013.0497

M3 - Article

VL - 369

SP - 1

EP - 4

JO - Philosophical Transactions of the Royal Society B: Biological Sciences

JF - Philosophical Transactions of the Royal Society B: Biological Sciences

SN - 0962-8436

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