Fit2d

Manufactured by Wavemetrics

Sourced in United States

Fit2D is a software tool designed to perform two-dimensional data fitting. It provides users with the ability to fit experimental data to various mathematical functions in a two-dimensional environment.

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Lab products found in correlation

Igor pro, by Wavemetrics (2 mentions) Igor pro version 6.22a, by Wavemetrics (1 mentions) Pilatus 100k, by Dectris (1 mentions) Pilatus3 1m, by Dectris (1 mentions) An60ti, by Beckman Coulter (1 mentions) Optima xl a, by Beckman Coulter (1 mentions)

3 protocols using fit2d

Synchrotron SAXS Characterization Protocol

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Synchrotron X-ray scattering data was collected at the Austrian SAXS beamline at ELETTRA (Trieste, Italy) [48 ]. Measurements were conducted at a wavelength of 0.154 nm and a sample-detector distance of 1.1 m. The photon energy was 8 keV. Data was recorded with a Pilatus detector (PILATUS 100K, DECTRIS Ltd., Villigen PSI, Switzerland), calibrated with silver behenate. The scattering intensity was measured as a function of the scattering vector q where

q = 4 π (\sin ϑ) ∕ λ

with 2ϑ being the scattering angle and λ being the wavelength. Samples were measured either in a 1.5 mm glass capillary (10-60 mM) or in a gel sample holder (75 mM). A discussion on the influence of shearing forces when filling the capillary can be found in the ESM (Table S7 and Fig. S8). Data analysis was done with Fit2D [49 ] and Igor Pro (Version 6.22A, WaveMetrics Inc., USA). Experimental intensities were normalized to the sample transmission and corrected for background. Absolute calibration was done by using water as secondary standard after the method described by Orthaber [50 ].

Kornmueller K., Letofsky-Papst I., Gradauer K., Mikl C., Cacho-Nerin F., Leypold M., Keller W., Leitinger G., Amenitsch H, & Prassl R. (2015). Tracking morphologies at the nanoscale: self-assembly of an amphiphilic designer peptide into a double helix superstructure. Nano research, 8(6), 1822-1833.

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Synchrotron X-ray Scattering Protocol

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Synchrotron X-ray scattering data was collected at the Austrian SAXS beamline at ELETTRA (Trieste, Italy) [37 (link)]. Measurements were conducted at a wavelength of 0.154 nm and a sample-detector distance of 1.1 m. The photon energy was 8 keV. The X-ray images were recorded with a Pilatus detector (Pilatus3 1M, DECTRIS Ltd., Villigen PSI, Switzerland), calibrated with silver behenate. The scattering intensity was measured as a function of the scattering vector q where

q = 4 π (\sin θ) / λ

with 2θ being the scattering angle and λ being the wavelength. Samples were measured in a 1.5 mm glass capillary. Data analysis was done with Fit2D [38 ] and Igor Pro (Version 6.22A, WaveMetrics Inc., USA). Experimental intensities were background corrected and absolute calibration was done with water as secondary standard, using the method described by Orthaber [39 ].

Kornmueller K., Lehofer B., Leitinger G., Amenitsch H, & Prassl R. (2017). Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures. Nano research, 11(2), 913-928.

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Biophysical Characterization of Ubiquitin Complexes

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All protein samples were dialyzed into their respective buffers (Ubc1 and Ubc1–Ub^Cys: 25 mM Tris-HCl, 1 mM EDTA, 150 mM NaCl at pH 7.5 (plus 2 mM TCEP for Ubc1); HIP2: 20 mM Tris-HCl, 200 mM NaCl, 1 mM TCEP at pH 8.0; HIP2–Ub^Cys: 25 mM Tris-HCl or 100 mM NaH₂PO₄, 400 mM NaCl, 1 mM EDTA at pH 7.5) and diluted with dialysis buffer to the desired experimental concentrations. Sedimentation equilibrium experiments were performed using a Beckman Optima XL-A analytical ultracentrifuge equipped with an An60Ti analytical rotor with six-channel Epon-charcoal centerpieces. Experiments were performed at 5°C using rotor speeds of 15, 18, 22 and 26,000 rpm and data was analyzed using a single ideal species model [21 (link)].
Small angle X-ray scattering (SAXS) data were collected at BioCAT Beamline ID-18 of the Advanced Photon Source (Argonne, Illinois) using X-rays with a wavelength of 1.03 Å. Data were recorded using a Brandeis II or Mar165 CCD detector with a sample to detector distance of 1892 mm to 2810 mm. Two dimensional images were radially integrated using either Fit2D [22 ] or Igor Pro (Wavemetrics, Lake Oswego, Oregon) and further processed using Microsoft Excel or the Igor Pro macros developed at BioCAT. CRYSOL [23 ] was used to calculate theoretical scattering from high-resolution atomic coordinates.

Cook B.W., Barber K.R., Shilton B.H, & Shaw G.S. (2015). The HIP2~Ubiquitin Conjugate Forms a Non-Compact Monomeric Thioester during Di-Ubiquitin Synthesis. PLoS ONE, 10(3), e0120318.

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