Application of in situ diffraction in high-throughput structure determination platforms

Pierre Aller; Juan Sanchez-Weatherby; James Foadi; Graeme Winter; Carina M C Lobley; Danny Axford; Alun W Ashton; Domenico Bellini; Jose Brandao-Neto; Simone Culurgioni; Alice Douangamath; Ramona Duman; Gwyndaf Evans; Stuart Fisher; Ralf Flaig; David R Hall; Petra Lukacik; Marco Mazzorana; Katherine E McAuley; Vitaliy Mykhaylyk; Robin L Owen; Neil G Paterson; Pierpaolo Romano; James Sandy; Thomas Sorensen; Frank von Delft; Armin Wagner; Anna Warren; Mark Williams; David I Stuart; Martin A Walsh

doi:10.1007/978-1-4939-2230-7_13

Application of in situ diffraction in high-throughput structure determination platforms

Pierre Aller, Juan Sanchez-Weatherby, James Foadi, Graeme Winter, Carina M C Lobley, Danny Axford, Alun W Ashton, Domenico Bellini, Jose Brandao-Neto, Simone Culurgioni, Alice Douangamath, Ramona Duman, Gwyndaf Evans, Stuart Fisher, Ralf Flaig, David R Hall, Petra Lukacik, Marco Mazzorana, Katherine E McAuley, Vitaliy MykhaylykRobin L Owen, Neil G Paterson, Pierpaolo Romano, James Sandy, Thomas Sorensen, Frank von Delft, Armin Wagner, Anna Warren, Mark Williams, David I Stuart, Martin A Walsh

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Review › Forskning › peer review

19 Citationer (Scopus)

Abstract

Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given.

Originalsprog	Engelsk
Tidsskrift	Methods in molecular biology (Clifton, N.J.)
Vol/bind	1261
Sider (fra-til)	233-53
Antal sider	21
ISSN	1064-3745
DOI	https://doi.org/10.1007/978-1-4939-2230-7_13
Status	Udgivet - 2015
Udgivet eksternt	Ja

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10.1007/978-1-4939-2230-7_13

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Aller, P., Sanchez-Weatherby, J., Foadi, J., Winter, G., Lobley, C. M. C., Axford, D., Ashton, A. W., Bellini, D., Brandao-Neto, J., Culurgioni, S., Douangamath, A., Duman, R., Evans, G., Fisher, S., Flaig, R., Hall, D. R., Lukacik, P., Mazzorana, M., McAuley, K. E., ... Walsh, M. A. (2015). Application of in situ diffraction in high-throughput structure determination platforms. Methods in molecular biology (Clifton, N.J.), 1261, 233-53. https://doi.org/10.1007/978-1-4939-2230-7_13

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title = "Application of in situ diffraction in high-throughput structure determination platforms",

abstract = "Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given. ",

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author = "Pierre Aller and Juan Sanchez-Weatherby and James Foadi and Graeme Winter and Lobley, {Carina M C} and Danny Axford and Ashton, {Alun W} and Domenico Bellini and Jose Brandao-Neto and Simone Culurgioni and Alice Douangamath and Ramona Duman and Gwyndaf Evans and Stuart Fisher and Ralf Flaig and Hall, {David R} and Petra Lukacik and Marco Mazzorana and McAuley, {Katherine E} and Vitaliy Mykhaylyk and Owen, {Robin L} and Paterson, {Neil G} and Pierpaolo Romano and James Sandy and Thomas Sorensen and {von Delft}, Frank and Armin Wagner and Anna Warren and Mark Williams and Stuart, {David I} and Walsh, {Martin A}",

year = "2015",

doi = "10.1007/978-1-4939-2230-7_13",

language = "English",

volume = "1261",

pages = "233--53",

journal = "Methods in molecular biology (Clifton, N.J.)",

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Aller, P, Sanchez-Weatherby, J, Foadi, J, Winter, G, Lobley, CMC, Axford, D, Ashton, AW, Bellini, D, Brandao-Neto, J, Culurgioni, S, Douangamath, A, Duman, R, Evans, G, Fisher, S, Flaig, R, Hall, DR, Lukacik, P, Mazzorana, M, McAuley, KE, Mykhaylyk, V, Owen, RL, Paterson, NG, Romano, P, Sandy, J, Sorensen, T, von Delft, F, Wagner, A, Warren, A, Williams, M, Stuart, DI & Walsh, MA 2015, 'Application of in situ diffraction in high-throughput structure determination platforms', Methods in molecular biology (Clifton, N.J.), bind 1261, s. 233-53. https://doi.org/10.1007/978-1-4939-2230-7_13

TY - JOUR

T1 - Application of in situ diffraction in high-throughput structure determination platforms

AU - Aller, Pierre

AU - Sanchez-Weatherby, Juan

AU - Foadi, James

AU - Winter, Graeme

AU - Lobley, Carina M C

AU - Axford, Danny

AU - Ashton, Alun W

AU - Bellini, Domenico

AU - Brandao-Neto, Jose

AU - Culurgioni, Simone

AU - Douangamath, Alice

AU - Duman, Ramona

AU - Evans, Gwyndaf

AU - Fisher, Stuart

AU - Flaig, Ralf

AU - Hall, David R

AU - Lukacik, Petra

AU - Mazzorana, Marco

AU - McAuley, Katherine E

AU - Mykhaylyk, Vitaliy

AU - Owen, Robin L

AU - Paterson, Neil G

AU - Romano, Pierpaolo

AU - Sandy, James

AU - Sorensen, Thomas

AU - von Delft, Frank

AU - Wagner, Armin

AU - Warren, Anna

AU - Williams, Mark

AU - Stuart, David I

AU - Walsh, Martin A

PY - 2015

Y1 - 2015

N2 - Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given.

AB - Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given.

KW - Automation, Laboratory

KW - Crystallography, X-Ray/instrumentation

KW - Macromolecular Substances/chemistry

KW - Proteomics/instrumentation

KW - Software

KW - Synchrotrons/instrumentation

U2 - 10.1007/978-1-4939-2230-7_13

DO - 10.1007/978-1-4939-2230-7_13

M3 - Review

C2 - 25502203

SN - 1064-3745

VL - 1261

SP - 233

EP - 253

JO - Methods in molecular biology (Clifton, N.J.)

JF - Methods in molecular biology (Clifton, N.J.)

ER -

Application of in situ diffraction in high-throughput structure determination platforms

Abstract

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