Literature DB >> 25537607

Upgrade of MacCHESS facility for X-ray scattering of biological macromolecules in solution.

Alvin Samuel Acerbo1, Michael J Cook1, Richard Edward Gillilan1.   

Abstract

X-ray scattering of biological macromolecules in solution is an increasingly popular tool for structural biology and benefits greatly from modern high-brightness synchrotron sources. The upgraded MacCHESS BioSAXS station is now located at the 49-pole wiggler beamline G1. The 20-fold improved flux over the previous beamline F2 provides higher sample throughput and autonomous X-ray scattering data collection using a unique SAXS/WAXS dual detectors configuration. This setup achieves a combined q-range from 0.007 to 0.7 Å(-1), enabling better characterization of smaller molecules, while opening opportunities for emerging wide-angle scattering methods. In addition, a facility upgrade of the positron storage ring to continuous top-up mode has improved beam stability and eliminated beam drift over the course of typical BioSAXS experiments. Single exposure times have been reduced to 2 s for 3.560 mg ml(-1) lysozyme with an average quality factor I/σ of 20 in the Guinier region. A novel disposable plastic sample cell design that incorporates lower background X-ray window material provides users with a more pristine sample environment than previously available. Systematic comparisons of common X-ray window materials bonded to the cell have also been extended to the wide-angle regime, offering new insight into best choices for various q-space ranges. In addition, a quantitative assessment of signal-to-noise levels has been performed on the station to allow users to estimate necessary exposure times for obtaining usable signals in the Guinier regime. Users also have access to a new BioSAXS sample preparation laboratory which houses essential wet-chemistry equipment and biophysical instrumentation. User experiments at the upgraded BioSAXS station have been on-going since commissioning of the beamline in Summer 2013. A planned upgrade of the G1 insertion device to an undulator for the Winter 2014 cycle is expected to further improve flux by an order of magnitude.

Keywords:  MacCHESS; SAXS; high throughput

Mesh:

Substances:

Year:  2015        PMID: 25537607      PMCID: PMC4294029          DOI: 10.1107/S1600577514020360

Source DB:  PubMed          Journal:  J Synchrotron Radiat        ISSN: 0909-0495            Impact factor:   2.616


  15 in total

1.  High-throughput biological small-angle X-ray scattering with a robotically loaded capillary cell.

Authors:  S S Nielsen; M Møller; R E Gillilan
Journal:  J Appl Crystallogr       Date:  2012-02-09       Impact factor: 3.304

Review 2.  Impact and progress in small and wide angle X-ray scattering (SAXS and WAXS).

Authors:  Melissa A Graewert; Dmitri I Svergun
Journal:  Curr Opin Struct Biol       Date:  2013-07-05       Impact factor: 6.809

3.  Characterization of a large glycoprotein proteoglycan by size-exclusion chromatography combined with light and X-ray scattering methods.

Authors:  Yasushi Watanabe; Yoji Inoko
Journal:  J Chromatogr A       Date:  2013-06-27       Impact factor: 4.759

4.  Accurate SAXS profile computation and its assessment by contrast variation experiments.

Authors:  Dina Schneidman-Duhovny; Michal Hammel; John A Tainer; Andrej Sali
Journal:  Biophys J       Date:  2013-08-20       Impact factor: 4.033

5.  Purification, crystallization, small-angle X-ray scattering and preliminary X-ray diffraction analysis of the SH2 domain of the Csk-homologous kinase.

Authors:  Natalie J Gunn; Michael A Gorman; Renwick C J Dobson; Michael W Parker; Terrence D Mulhern
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-02-23

6.  Breaking the radiation damage limit with Cryo-SAXS.

Authors:  Steve P Meisburger; Matthew Warkentin; Huimin Chen; Jesse B Hopkins; Richard E Gillilan; Lois Pollack; Robert E Thorne
Journal:  Biophys J       Date:  2013-01-08       Impact factor: 4.033

7.  Radiation damage to a protein solution, detected by synchrotron X-ray small-angle scattering: dose-related considerations and suppression by cryoprotectants.

Authors:  Shigeo Kuwamoto; Shuji Akiyama; Tetsuro Fujisawa
Journal:  J Synchrotron Radiat       Date:  2004-10-22       Impact factor: 2.616

8.  Characterization of proteins with wide-angle X-ray solution scattering (WAXS).

Authors:  Lee Makowski
Journal:  J Struct Funct Genomics       Date:  2010-01-05

9.  Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam.

Authors:  Rita Graceffa; R Paul Nobrega; Raul A Barrea; Sagar V Kathuria; Srinivas Chakravarthy; Osman Bilsel; Thomas C Irving
Journal:  J Synchrotron Radiat       Date:  2013-10-01       Impact factor: 2.616

10.  Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33.

Authors:  A R Round; D Franke; S Moritz; R Huchler; M Fritsche; D Malthan; R Klaering; D I Svergun; M Roessle
Journal:  J Appl Crystallogr       Date:  2008-08-16       Impact factor: 3.304

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  38 in total

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Authors:  Janice M Reimer; Martin N Aloise; Paul M Harrison; T Martin Schmeing
Journal:  Nature       Date:  2016-01-14       Impact factor: 49.962

2.  The GlcN6P cofactor plays multiple catalytic roles in the glmS ribozyme.

Authors:  Jamie L Bingaman; Sixue Zhang; David R Stevens; Neela H Yennawar; Sharon Hammes-Schiffer; Philip C Bevilacqua
Journal:  Nat Chem Biol       Date:  2017-02-13       Impact factor: 15.040

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Authors:  Po-Chia Chen; Janosch Hennig
Journal:  Biophys Rev       Date:  2018-10-10

4.  Predicting X-ray solution scattering from flexible macromolecules.

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Journal:  Protein Sci       Date:  2018-10-16       Impact factor: 6.725

5.  The consequences of cavity creation on the folding landscape of a repeat protein depend upon context.

Authors:  Kelly A Jenkins; Martin J Fossat; Siwen Zhang; Durgesh K Rai; Sean Klein; Richard Gillilan; Zackary White; Grayson Gerlich; Scott A McCallum; Roland Winter; Sol M Gruner; Doug Barrick; Catherine A Royer
Journal:  Proc Natl Acad Sci U S A       Date:  2018-08-13       Impact factor: 11.205

Review 6.  Predicting data quality in biological X-ray solution scattering.

Authors:  Chenzheng Wang; Yuexia Lin; Devin Bougie; Richard E Gillilan
Journal:  Acta Crystallogr D Struct Biol       Date:  2018-07-24       Impact factor: 7.652

7.  The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.

Authors:  Crystal A Khan; Steve P Meisburger; Nozomi Ando; Paul F Fitzpatrick
Journal:  J Biol Chem       Date:  2019-01-23       Impact factor: 5.157

8.  Quantifying radiation damage in biomolecular small-angle X-ray scattering.

Authors:  Jesse B Hopkins; Robert E Thorne
Journal:  J Appl Crystallogr       Date:  2016-05-04       Impact factor: 3.304

9.  Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.

Authors:  Rory C Henderson; Feng Gao; Srinivas Jayanthi; Alicia Kight; Priyanka Sharma; Robyn L Goforth; Colin D Heyes; Ralph L Henry; Thallapuranam Krishnaswamy Suresh Kumar
Journal:  Biophys J       Date:  2016-09-20       Impact factor: 4.033

10.  7-Phenoxy-Substituted 3,4-Dihydro-2H-1,2,4-benzothiadiazine 1,1-Dioxides as Positive Allosteric Modulators of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors with Nanomolar Potency.

Authors:  Eric Goffin; Thomas Drapier; Anja Probst Larsen; Pierre Geubelle; Christopher P Ptak; Saara Laulumaa; Karoline Rovinskaja; Julie Gilissen; Pascal de Tullio; Lars Olsen; Karla Frydenvang; Bernard Pirotte; Julien Hanson; Robert E Oswald; Jette Sandholm Kastrup; Pierre Francotte
Journal:  J Med Chem       Date:  2017-12-19       Impact factor: 7.446

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