A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler

Michele Cianci; Svetlana Antonyuk; Neil Bliss; Mike W. Bailey; Stephen G. Buffey; Kan C. Cheung; Jim A. Clarke; Gareth E. Derbyshire; Mark J. Ellis; Mark J. Enderby; Alan F. Grant; Martin P. Holbourn; David Laundy; Colin Nave; Roy Ryder; Paul Stephenson; John R. Helliwell; S. Samar Hasnain

doi:10.1107/S0909049505009131

A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler

Michele Cianci, Svetlana Antonyuk, Neil Bliss, Mike W. Bailey, Stephen G. Buffey, Kan C. Cheung, Jim A. Clarke, Gareth E. Derbyshire, Mark J. Ellis, Mark J. Enderby, Alan F. Grant, Martin P. Holbourn, David Laundy, Colin Nave, Roy Ryder, Paul Stephenson, John R. Helliwell, S. Samar Hasnain

Research output: Contribution to journal › Article › peer-review

Abstract

The North West Structural Genomics Centre's beamline, MAD10, at the SRS receives the central part of the radiation fan (0.5 mrad vertically, 4 mrad horizontally) produced by a new 2.46 T ten-pole wiggler. The optical arrangement of the beamline consists of a Rh-coated collimating Si mirror, a fixed-exit-beam double-crystal monochromator with sagittal bending for horizontal focusing and a second Rh-coated Si mirror for vertical focusing. The double-crystal Si (111) monochromator allows data collection in the 5-13.5 keV photon energy range with rapid (subsecond) tunability and high energy resolution. The monochromatic beam is optimized through a 200 μm collimator. The beamline end station has been designed around a Mar desktop beamline with high-throughput cryogenic sample changer, Mar225 CCD detector, liquid-N 2 autofill system and an ORTEC C-TRAIN-04 energy-resolving high-count-rate X-ray fluorescence detector. The instrument is optimized for MAD/SAD applications in protein crystallography with the additional mode of operation of online single-crystal EXAFS studies on the same crystals. Thus, screening of metals/Se in the crystal can be performed quickly prior to MAD/SAD data collection by exciting the crystal with X-rays of appropriate energy and recording an energy-dispersive fluorescence spectrum. In addition, this experimental set-up allows for parallel XAFS measurements on the same crystal to monitor 'radiation-induced' changes, if any, in e.g. the redox state of metal centres to be detected for a 'metallic' functional group during crystallographic data collection. Moreover, careful minimization of the thickness of the Be window maximizes the intensity performance for the 2.0-2.5 Å softer wavelength range. This range also covers the K-edges of a number of important 3d transition metals as well as the L-edges of xenon and iodine and enhanced sulfur f″. © 2005 International Union of Crystallography Printed in Great Britain - All rights reserved.

Original language	English
Pages (from-to)	455-466
Number of pages	11
Journal	Journal of Synchrotron Radiation
Volume	12
Issue number	4
DOIs	https://doi.org/10.1107/S0909049505009131
Publication status	Published - Jul 2005

Keywords

High throughput
Macromolecular crystallography
MAD
Metalloprotein
SAD
Single-crystal EXAFS
Softer x-rays
Structural genomics
X-ray fluorescence

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10.1107/S0909049505009131

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Cianci, M., Antonyuk, S., Bliss, N., Bailey, M. W., Buffey, S. G., Cheung, K. C., Clarke, J. A., Derbyshire, G. E., Ellis, M. J., Enderby, M. J., Grant, A. F., Holbourn, M. P., Laundy, D., Nave, C., Ryder, R., Stephenson, P., Helliwell, J. R., & Hasnain, S. S. (2005). A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler. Journal of Synchrotron Radiation, 12(4), 455-466. https://doi.org/10.1107/S0909049505009131

@article{5a95b16464e04f7ba737c403491043aa,

title = "A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler",

abstract = "The North West Structural Genomics Centre's beamline, MAD10, at the SRS receives the central part of the radiation fan (0.5 mrad vertically, 4 mrad horizontally) produced by a new 2.46 T ten-pole wiggler. The optical arrangement of the beamline consists of a Rh-coated collimating Si mirror, a fixed-exit-beam double-crystal monochromator with sagittal bending for horizontal focusing and a second Rh-coated Si mirror for vertical focusing. The double-crystal Si (111) monochromator allows data collection in the 5-13.5 keV photon energy range with rapid (subsecond) tunability and high energy resolution. The monochromatic beam is optimized through a 200 μm collimator. The beamline end station has been designed around a Mar desktop beamline with high-throughput cryogenic sample changer, Mar225 CCD detector, liquid-N 2 autofill system and an ORTEC C-TRAIN-04 energy-resolving high-count-rate X-ray fluorescence detector. The instrument is optimized for MAD/SAD applications in protein crystallography with the additional mode of operation of online single-crystal EXAFS studies on the same crystals. Thus, screening of metals/Se in the crystal can be performed quickly prior to MAD/SAD data collection by exciting the crystal with X-rays of appropriate energy and recording an energy-dispersive fluorescence spectrum. In addition, this experimental set-up allows for parallel XAFS measurements on the same crystal to monitor 'radiation-induced' changes, if any, in e.g. the redox state of metal centres to be detected for a 'metallic' functional group during crystallographic data collection. Moreover, careful minimization of the thickness of the Be window maximizes the intensity performance for the 2.0-2.5 {\AA} softer wavelength range. This range also covers the K-edges of a number of important 3d transition metals as well as the L-edges of xenon and iodine and enhanced sulfur f″. {\textcopyright} 2005 International Union of Crystallography Printed in Great Britain - All rights reserved.",

keywords = "High throughput, Macromolecular crystallography, MAD, Metalloprotein, SAD, Single-crystal EXAFS, Softer x-rays, Structural genomics, X-ray fluorescence",

author = "Michele Cianci and Svetlana Antonyuk and Neil Bliss and Bailey, {Mike W.} and Buffey, {Stephen G.} and Cheung, {Kan C.} and Clarke, {Jim A.} and Derbyshire, {Gareth E.} and Ellis, {Mark J.} and Enderby, {Mark J.} and Grant, {Alan F.} and Holbourn, {Martin P.} and David Laundy and Colin Nave and Roy Ryder and Paul Stephenson and Helliwell, {John R.} and Hasnain, {S. Samar}",

year = "2005",

month = jul,

doi = "10.1107/S0909049505009131",

language = "English",

volume = "12",

pages = "455--466",

journal = "Journal of Synchrotron Radiation",

issn = "0909-0495",

publisher = "International Union of Crystallography",

number = "4",

}

Cianci, M, Antonyuk, S, Bliss, N, Bailey, MW, Buffey, SG, Cheung, KC, Clarke, JA, Derbyshire, GE, Ellis, MJ, Enderby, MJ, Grant, AF, Holbourn, MP, Laundy, D, Nave, C, Ryder, R, Stephenson, P, Helliwell, JR & Hasnain, SS 2005, 'A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler', Journal of Synchrotron Radiation, vol. 12, no. 4, pp. 455-466. https://doi.org/10.1107/S0909049505009131

TY - JOUR

T1 - A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler

AU - Cianci, Michele

AU - Antonyuk, Svetlana

AU - Bliss, Neil

AU - Bailey, Mike W.

AU - Buffey, Stephen G.

AU - Cheung, Kan C.

AU - Clarke, Jim A.

AU - Derbyshire, Gareth E.

AU - Ellis, Mark J.

AU - Enderby, Mark J.

AU - Grant, Alan F.

AU - Holbourn, Martin P.

AU - Laundy, David

AU - Nave, Colin

AU - Ryder, Roy

AU - Stephenson, Paul

AU - Helliwell, John R.

AU - Hasnain, S. Samar

PY - 2005/7

Y1 - 2005/7

N2 - The North West Structural Genomics Centre's beamline, MAD10, at the SRS receives the central part of the radiation fan (0.5 mrad vertically, 4 mrad horizontally) produced by a new 2.46 T ten-pole wiggler. The optical arrangement of the beamline consists of a Rh-coated collimating Si mirror, a fixed-exit-beam double-crystal monochromator with sagittal bending for horizontal focusing and a second Rh-coated Si mirror for vertical focusing. The double-crystal Si (111) monochromator allows data collection in the 5-13.5 keV photon energy range with rapid (subsecond) tunability and high energy resolution. The monochromatic beam is optimized through a 200 μm collimator. The beamline end station has been designed around a Mar desktop beamline with high-throughput cryogenic sample changer, Mar225 CCD detector, liquid-N 2 autofill system and an ORTEC C-TRAIN-04 energy-resolving high-count-rate X-ray fluorescence detector. The instrument is optimized for MAD/SAD applications in protein crystallography with the additional mode of operation of online single-crystal EXAFS studies on the same crystals. Thus, screening of metals/Se in the crystal can be performed quickly prior to MAD/SAD data collection by exciting the crystal with X-rays of appropriate energy and recording an energy-dispersive fluorescence spectrum. In addition, this experimental set-up allows for parallel XAFS measurements on the same crystal to monitor 'radiation-induced' changes, if any, in e.g. the redox state of metal centres to be detected for a 'metallic' functional group during crystallographic data collection. Moreover, careful minimization of the thickness of the Be window maximizes the intensity performance for the 2.0-2.5 Å softer wavelength range. This range also covers the K-edges of a number of important 3d transition metals as well as the L-edges of xenon and iodine and enhanced sulfur f″. © 2005 International Union of Crystallography Printed in Great Britain - All rights reserved.

AB - The North West Structural Genomics Centre's beamline, MAD10, at the SRS receives the central part of the radiation fan (0.5 mrad vertically, 4 mrad horizontally) produced by a new 2.46 T ten-pole wiggler. The optical arrangement of the beamline consists of a Rh-coated collimating Si mirror, a fixed-exit-beam double-crystal monochromator with sagittal bending for horizontal focusing and a second Rh-coated Si mirror for vertical focusing. The double-crystal Si (111) monochromator allows data collection in the 5-13.5 keV photon energy range with rapid (subsecond) tunability and high energy resolution. The monochromatic beam is optimized through a 200 μm collimator. The beamline end station has been designed around a Mar desktop beamline with high-throughput cryogenic sample changer, Mar225 CCD detector, liquid-N 2 autofill system and an ORTEC C-TRAIN-04 energy-resolving high-count-rate X-ray fluorescence detector. The instrument is optimized for MAD/SAD applications in protein crystallography with the additional mode of operation of online single-crystal EXAFS studies on the same crystals. Thus, screening of metals/Se in the crystal can be performed quickly prior to MAD/SAD data collection by exciting the crystal with X-rays of appropriate energy and recording an energy-dispersive fluorescence spectrum. In addition, this experimental set-up allows for parallel XAFS measurements on the same crystal to monitor 'radiation-induced' changes, if any, in e.g. the redox state of metal centres to be detected for a 'metallic' functional group during crystallographic data collection. Moreover, careful minimization of the thickness of the Be window maximizes the intensity performance for the 2.0-2.5 Å softer wavelength range. This range also covers the K-edges of a number of important 3d transition metals as well as the L-edges of xenon and iodine and enhanced sulfur f″. © 2005 International Union of Crystallography Printed in Great Britain - All rights reserved.

KW - High throughput

KW - Macromolecular crystallography

KW - MAD

KW - Metalloprotein

KW - SAD

KW - Single-crystal EXAFS

KW - Softer x-rays

KW - Structural genomics

KW - X-ray fluorescence

U2 - 10.1107/S0909049505009131

DO - 10.1107/S0909049505009131

M3 - Article

SN - 0909-0495

VL - 12

SP - 455

EP - 466

JO - Journal of Synchrotron Radiation

JF - Journal of Synchrotron Radiation

IS - 4

ER -

A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler

Abstract

Keywords

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