Synchrotron SAXS data from solutions of ATP-dependent Clp protease ATP-binding subunit ClpC1 (second state) in 50 mM HEPES, pH 7.5, 100 mM KCl, 10% v/v glycerol, 4 mM MgCl2 and 1 mM ATP were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SEC-SAXS was performed on a sample at at 20°C. 50 successive 1 second frames were collected through the corresponding SEC elution peak. Each data frame was normalized to the intensity of the transmitted beam and radially averaged (2D- to 1D data reduction). The scattering of the solvent-blank (reduced data obtained from the elution buffer) was subtracted from each sample frame and the resulting subtracted SAXS profiles were scaled and averaged to generate the data displayed in this entry.
相关论文
标题
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from <i>Mycobacterium tuberculosis</i>.
作者
Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from <i>Mycobacterium tuberculosis</i>.
project.publication.title
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from <i>Mycobacterium tuberculosis</i>.
project.publication.author_list
Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H
European Molecular Biology Laboratory (EMBL) - Grenoble Outstation
experiment.contributor[0].affiliation[0].webpage
https://www.embl.fr/
experiment.contributor[0].contributor_name
Martha
experiment.contributor[0].contributor_surname
Brennich
experiment.contributor[0].orcid
null
experiment.concentration_method
null
experiment.concentration_unit
null
experiment.date
2017-09-18
experiment.storage_temperature
20.0
experiment.cell_temperature
20.0
experiment.exposure_time
1.0
experiment.number_of_frames
50
experiment.wavelength
0.099
experiment.sample_detector_distance
2.867
experiment.concentration_min
null
experiment.concentration_max
null
experiment.sample_volume
null
experiment.flow_rate
null
experiment.s_min
0.095
experiment.s_max
1.443
experiment.total_exposure_time
null
experiment.seccolumn
null
fits
[]
estimated_volume_method
null
pddf_software
ATSAS GNOM
pddf_software_version
5.0
i0_calibration_standard
null
description
null
experiment_description
Synchrotron SAXS data from solutions of ATP-dependent Clp protease ATP-binding subunit ClpC1 (second state) in 50 mM HEPES, pH 7.5, 100 mM KCl, 10% v/v glycerol, 4 mM MgCl2 and 1 mM ATP were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SEC-SAXS was performed on a sample at at 20°C. 50 successive 1 second frames were collected through the corresponding SEC elution peak. Each data frame was normalized to the intensity of the transmitted beam and radially averaged (2D- to 1D data reduction). The scattering of the solvent-blank (reduced data obtained from the elution buffer) was subtracted from each sample frame and the resulting subtracted SAXS profiles were scaled and averaged to generate the data displayed in this entry.
