Dataset for "Ensilicated tetanus antigen retains immunogenicity: in vivo study and time-resolved SAXS characterization"

771 56 13044 3 38885 document 13044 Figure 1 - in vivo and CD.rar application/x-rar 0652a13d02171b37d90f248d9490f702 MD5 560368 2020-03-03 12:17:54 https://researchdata.bath.ac.uk/771/1/Figure%201%20-%20in%20vivo%20and%20CD.rar 771 1 1 application/x-rar other Circular Dichroism thermal stability and ELISA in vivo study data for TTCF SAXS paper en public cc_by

Figure 1 - in vivo and CD.rar

data 13045 3 38887 document 13045 Figure 2 - ESRF data.rar application/x-rar 19d2ab0c0e1fe6c781aa9eea83bd1aba MD5 683789811 2020-03-03 12:19:58 https://researchdata.bath.ac.uk/771/2/Figure%202%20-%20ESRF%20data.rar 771 2 2 application/x-rar other ESRF SAXS data obtained at beamline ID02 for TTCF. en public cc_by

Figure 2 - ESRF data.rar

data 13046 3 38889 document 13046 Figure 3 - Diamond data.rar application/x-rar 7ea768ae964d166818d2c3b9aabf8193 MD5 2811573925 2020-03-03 12:22:58 https://researchdata.bath.ac.uk/771/3/Figure%203%20-%20Diamond%20data.rar 771 3 3 application/x-rar other Diamond SAXS data obtained at beamline I22 for TTCF en public cc_by

Figure 3 - Diamond data.rar

data 13047 3 38891 document 13047 Figure 4 - Overview image.rar application/x-rar 76a0067172a318e4db1258e8e3a5fa95 MD5 37544492 2020-03-03 12:26:23 https://researchdata.bath.ac.uk/771/4/Figure%204%20-%20Overview%20image.rar 771 4 4 application/x-rar other Overview figure 4 presentation en public cc_by

Figure 4 - Overview image.rar

data 13048 3 38893 document 13048 Supplementary.rar application/x-rar 584bc976affefdeba38ffffc101f788a MD5 3573603 2020-03-03 12:26:51 https://researchdata.bath.ac.uk/771/5/Supplementary.rar 771 5 5 application/x-rar other All data for the figures used in the supplementary en public cc_by

Supplementary.rar

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run numbers + samples_updated_AD.xlsx

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log.pdf

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http://eprints.org/relation/isVersionOf https://researchdata.bath.ac.uk/id/document/13050 http://eprints.org/relation/isVolatileVersionOf https://researchdata.bath.ac.uk/id/document/13050 http://eprints.org/relation/issmallThumbnailVersionOf https://researchdata.bath.ac.uk/id/document/13050 archive 6765 disk0/00/00/07/71 2020-06-12 08:35:54 2024-07-18 12:31:56 2020-06-12 08:35:54 data_collection show Doekhie Aswin A.Doekhie@bath.ac.uk 0000-0002-9612-7588 University of Bath TRUE Sartbaeva Asel A.Sartbaeva@bath.ac.uk 0000-0003-1017-0161 University of Bath TRUE Koumanov Francoise F.Koumanov@bath.ac.uk 0000-0002-9029-3390 University of Bath FALSE Van Den Elsen Jean J.M.H.V.Elsen@bath.ac.uk 0000-0002-0367-1956 University of Bath FALSE Edler Karen K.Edler@bath.ac.uk 0000-0001-5822-0127 University of Bath FALSE Wells Stephen S.A.Wells@bath.ac.uk 0000-0002-3920-3644 University of Bath FALSE Dataset for "Ensilicated tetanus antigen retains immunogenicity: in vivo study and time-resolved SAXS characterization" BV0030 BY0020 BY0050 BY0100 BY0110 BY0120 CA0040 CG0010 GE0040 GS0010 GS0080 GV0040 HH0010 dept_chem SAXS, thermal stability, tetanus, vaccine, cold chain, time-resolved, protein, silica, sol-gel, ensilication Data are stored per figure presented in the original work and supplementary information. MatLab code is supplemented for generating figures. This dataset contains the SAXS data obtained at i22 (Diamond Light Source) and ID02 beamline (ESRF). Other data such as ELISA and Circular Dichroism are also included. All data is organised by figures presented in the research paper. Majority of data is stored in excel or csv format with processing done in MatLab for graphical presentation. 2020-06-08 University of Bath public RightsHolder University of Bath Annett Trust EH-CH1283 PhD Studentship University of Bath https://doi.org/10.13039/501100000835 Medical Research Council https://doi.org/10.13039/501100000265 MR/P002927/1 Role of Rab3 in Peripheral Tissue Insulin Resistance Royal Society https://doi.org/10.13039/501100000288 UF140623 Royal Society University Research Fellowship (Asel Sartbaeva) – Renewal Diamond Light Source https://doi.org/10.13039/100011889 SM-14148 Thermally stabilised proteins: in situ protein ensilication European Synchrotron Radiation Facility https://doi.org/10.13039/501100001671 SC4282 Thermally stabilised proteins: in situ ensilication Biotechnology and Biological Sciences Research Council https://doi.org/10.13039/501100000268 BB/N022165/1 Improved Conjugate Vaccines Derived from a Bacterial Immunomodulatory Protein European Research Council https://doi.org/10.13039/501100000781 648283 GROWMOF – Modelling of MOF Self-Assembly, Crystal Growth and Thin Film Formation Time-resolved (ultra) SAXS (ID02, ESRF): Small Angle X-Ray Scattering (SAXS)21 measurements were performed on the Time-Resolved Ultra Small-Angle Scattering beamline ID02 at the ESRF, Grenoble, France. The incident X-ray energy was 12.46 keV and two sample-detector distances were employed: 1.5 m (SAXS) and 10 m (USAXS). SAXS data were acquired using the Rayonix MX-170HS detector with exposure times between 0.01 and 0.03 seconds at room temperature (20 °C). Pre-hydrolysed TEOS was added to 10 ml of 1 mg/ml TTCF solution at 1:50 (v/v) ratio at pH 7 ex situ, initiating the ensilication reaction. Using a sterile syringe, 1 ml of this ensilication mixture was injected into a quartz capillary (figure S2) after which the beamline hutch was checked for safety and closed for the start of measurement. We measured the delay on hutch closure to be approximately 1 minute. As a result, the total time delay between the start of the reaction and the first measurements was between 1 and 2 minutes. The measured 2D patterns, after normalisation by incident flux, sample transmission, and solid angle, were azimuthally averaged to obtain the 1D static scattering profiles as a function of the magnitude of the scattering vector q=4π/λ sin(θ/2), with λ the incident X-ray wavelength (=0.996 Å-1) and θ the scattering angle. This gave two overlapping q-ranges of 0.0008≤q≤0.008 and 0.006≤q≤0.5 Å-1. The scattering background in each case was measured using Tris buffer and the normalised background subtracted data are represented by I(q). Fitting of SAXS data: Data fitting was done using several models within SASview to probe the various changes observed in the scattering signal. Good residual fits were found using a combination of power law, ellipsoid, broad peak and mass fractal models at different stages of the ensilication process. The ellipsoid model provided shape information (the polar and equatorial radii, Rpolar and Requatorial respectively) on the protein and the initial growth of its silica coating. The broad peak model gave a characteristic length scale for scattering consistent with the particle sizes from the ellipsoid fits, and was utilised as a transition model towards the mass fractal growth. The latter provided the fractal radius of silica particulates and fractal dimension, Rfrac and Df respectively, which are indicative of reaction type. All models were assessed on χ2 as a goodness-of-fit indicator. Detailed information about the fitting parameters are presented in the Supplementary Information. in situ time-resolved SAXS (i22, Diamond Light Source): Small Angle X-Ray Scattering (SAXS) measurements during ensilication in situ were performed on the Time-Resolved Small-Angle Scattering beamline i22 at Diamond Light Source, Didcot, UK. TTCF at 1 mg/ml in (50 mM Tris pH 7.0) buffer, 25 ml volume, was circulated using a peristaltic pump at 2 ml / min through Teflon tubing with an internal diameter of 1.6 mm. The sample solution passed through a 1.5 mm capillary flow cell in a loop before addition of hydrolysed TEOS via a syringe injector. Both pump and injector were remotely controlled (figure S3). SAXS frames were taken at 1 frame/sec for 120 seconds. Pre-hydrolysed TEOS was added to the sample at 1:50 (v/v) ratio after 3 seconds from start of measurement, so that data on the native protein could be acquired before ensilication began. The incident X-ray energy was 12.4 keV. SAXS data were acquired using the Pilatus P3-2M detector at 2.2 m sample distance with 0.8 seconds exposure time. The collected 2D data were processed using a pipeline setup in the Data Analysis WorkbeNch (DAWN) software27. The pipeline was set up with detector calibration, SAXS mask, Poisson error, time with flux and transmission correction. Azimuthal integration produced 1D data in I vs q, where q=4π/λ sin(θ/2), with λ the incident X-ray wavelength (0.9998 Å) and θ the scattering angle. The q range was between 0.008≤q≤0.75 Å-1. The experiment was performed at room temperature (20 °C). Background subtraction scattering was done using a double subtraction method (figure S4 & table S1). Empty capillary scattering was subtracted from Tris buffer scattering. The sample SAXS was then processed by subtracting Tris buffer (minus capillary scattering) and capillary scattering only (table S1). Diamond Light Source data was processed via DAWN. ESRF data was processed using SAXSutilities. SASview was used to analyse the datasets. en 1 10.15125/BATH-00771 https://doi.org/10.1038/s41598-020-65876-3 pub open