cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.7956041.v1
title: Supplementary Figure 20 Average size of particle formed by pY-AtzA and super-binder AtzC-SH2

description: Article: Stimulus-responsive Self-Assembly of Protein-Based Fractals by Computational Design Pre-print: bioRxiv 274183; doi: https://doi.org/10.1101/274183 Figure: Fig. S20. Average size of particle formed by pY-AtzA and super-binder AtzC-SH2. (A) Heat map showing volume-weighted mean size of particles found from 50-3000 nM pY-AtzA and 50-2000 nM AtzC-SH2. Value shown is average of two physical samples. Histogram illustrates distribution of sizes found on heatmap. (B) Volume distributions of heat map. Distributions shown are representative of other traces in the sample. (SI 2.9) Phosphorylation, assembly formation, and disassembly – The phosphorylation protocol was based upon Src kinase activity assay by Sigma (Catalog # S1076). In a final reaction volume of 150μL, 3μM AtzAM1 was mixed into 1X Kinase Activity Buffer (4mM MgCl2, 2.5mM MnCl2, 0.25mM DTT, 5mM MOPS, 2.5mM glycerol-2-phosphate, 1mM EGTA, 400nM EDTA, pH 7.6), 2.5 mM MnCl2,HNG, 2 mM ATP, 800ng Src kinase, and incubated for 7 – 16 hr at 25°C for phosphorylation to occur. After phosphorylating, AtzCM1 was added to a final 2μM concentration. Assembly was allowed to form at 2hr 25°C. Disassembly was performed by adding 4.8μg of YopH phosphatase into the 150μL reaction mixture after assembly formation occurred. Size measurements using DLS were performed to determine assembly formation/disassembly. (SI 2.10) Dynamic light scattering (DLS) – 50 μL of an assembly sample was used for size determination using a Malvern Zetasizer and a quartz cuvette (ZEN2112, Malvern). Ten spectra measures were recorded for eleven replicates at 25 °C. The standard operating procedure accounted for 5% glycerol in solution. % volume was collected and reported. (SI 2.12) DLS Titration Experiment – 6 µM, 3 µM, 1.5 µM, 0.5 µM, 0.1 µM pyAtzA was phosphorylated (as described previously) with an incubation time of overnight at 25°C. Either AtzCM1 wildtype (WT) or AtzCM1 superbinder (SB) was added to each sample at 2 µM, 1 µM, 0.5 µM, 0.25 µM, 0.50 µM final concentration. The sample was allowed to incubate for 2 hr at 25°C. Therefore, the final concentrations of all components was from 3 µM – 0.05 µM pyAtzA, 2 µM – 0.05 µM AtzCM1-WT or AtzCM1-SB. DLS was performed at 25°C, 50 µL/sample volume, in a low-volume quartz sizing cuvette (Malvern; ZEN2112) using a Zetasizer Nano ZS (Malvern). Measurements were performed in duplicate with each sample read and averaged 15 times.<br>
DOI: 10.6084/m9.figshare.7956194.v4
title: Table S2 - WGS and RNAseq summary information

description: Whole-genome sequencing and RNA sequencing summary information.
DOI: 10.6084/m9.figshare.7956026
title: Supplementary Figure 7 Phosphorylation of SH2 peptide AtzA fusion (pY-AtzA) by Src kinase

description: Article: Stimulus-responsive Self-Assembly of Protein-Based Fractals by Computational Design Pre-print: bioRxiv 274183; doi: https://doi.org/10.1101/274183 Figure: S7. Phosphorylation of SH2 peptide AtzA fusion (pY-AtzA) by Src kinase. In order to verify phosphorylation of AtzA by Src kinase into phosphorylated SH2 peptide AtzA fusion (pY-AtzA), ELISA with (1:4000 dilution) antiphosphotyrosine-horseradish peroxidase conjugate was performed on pY-AtzA samples either with Src kinase (+) or without Src kinase (-), in phosphorylation reaction buffer at 1.25 µg/mL pY-AtzA or 20 µg/mL pY-AtzA. Data is presented as mean ± 1 standard deviation. (SI 2.9) Phosphorylation, assembly formation, and disassembly – The phosphorylation protocol was based upon Src kinase activity assay by Sigma (Catalog # S1076). In a final reaction volume of 150μL, 3μM AtzAM1 was mixed into 1X Kinase Activity Buffer (4mM MgCl2, 2.5mM MnCl2, 0.25mM DTT, 5mM MOPS, 2.5mM glycerol-2-phosphate, 1mM EGTA, 400nM EDTA, pH 7.6), 2.5 mM MnCl2,HNG, 2 mM ATP, 800ng Src kinase, and incubated for 7 – 16 hr at 25°C for phosphorylation to occur. After phosphorylating, AtzCM1 was added to a final 2μM concentration. Assembly was allowed to form at 2hr 25°C. Disassembly was performed by adding 4.8μg of YopH phosphatase into the 150μL reaction mixture after assembly formation occurred. Size measurements using DLS were performed to determine assembly formation/disassembly. (SI 2.7) Enzyme-linked immunosorbent assay (ELISA) – Phosphorylated AtzAM1 (pY27 AtzAM1) was loaded onto clear flat-bottom immuno 96-well plates (Thermo Scientific item #442404) at 20μg/mL and 1.25μg/mL in 50μL 1X PBS (Gibco pH 7.4, #10010023) overnight at 4◦C. Plates were rinsed twice in 200μL 1X TBS (Biorad #1706435). 1% BSA in TBS 0.05% Tween 20 was used to block wells at 200μL block solution for 1.5hr at 25°C under gentle agitation. Anti-phosphotyrosine 4G10 Platinum HRP conjugate (EMD #16-316) was diluted 1:5000 in 1% BSA TBS 0.05% Tween 20 and loaded onto the well at 25°C for 1.5hr under gentle agitation. Excess anti-phosphotyrosine was washed off with 200μL of TBS 0.05% Tween 20 in triplicate. To detect bound antibody, 100μL of TMB substrate reagent (Biolegend #421101) was added to each well and incubated for 5 minutes at 25°C. 100μL of TMB stop solution (Biolegend #423001) was added to the wells. Absorbance was read at 450nm using the Tecan Infinite M200 Pro plate reader.****Note: This work was part of the <b>Rutgers Biomod 2016 </b>project (M. Liu, A. Permaul, O. Dineen, M. Khalid, M. Shea, G.L. Bilker). See reference for additional details.
DOI: 10.6084/m9.figshare.7956032
title: Supplementary Figure 19 Average size of particle formed by pY-AtzA and wild type AtzC-SH2

description: Article: Stimulus-responsive Self-Assembly of Protein-Based Fractals by Computational Design Pre-print: bioRxiv 274183; doi: https://doi.org/10.1101/274183 Figure: S19. Average size of particle formed by pY-AtzA and wild type AtzC-SH2. (A) Heat map showing volume-weighted mean size of particles found from 50-3000 nM pY-AtzA and 50-2000 nM AtzC-SH2. Value shown is average of two physical samples. Histogram illustrates distribution of sizes found on heatmap. (B) Volume distributions of heat map. Distributions shown are representative of other traces in the sample. (SI 2.9) Phosphorylation, assembly formation, and disassembly – The phosphorylation protocol was based upon Src kinase activity assay by Sigma (Catalog # S1076). In a final reaction volume of 150μL, 3μM AtzAM1 was mixed into 1X Kinase Activity Buffer (4mM MgCl2, 2.5mM MnCl2, 0.25mM DTT, 5mM MOPS, 2.5mM glycerol-2-phosphate, 1mM EGTA, 400nM EDTA, pH 7.6), 2.5 mM MnCl2,HNG, 2 mM ATP, 800ng Src kinase, and incubated for 7 – 16 hr at 25°C for phosphorylation to occur. After phosphorylating, AtzCM1 was added to a final 2μM concentration. Assembly was allowed to form at 2hr 25°C. Disassembly was performed by adding 4.8μg of YopH phosphatase into the 150μL reaction mixture after assembly formation occurred. Size measurements using DLS were performed to determine assembly formation/disassembly. (SI 2.10) Dynamic light scattering (DLS) – 50 μL of an assembly sample was used for size determination using a Malvern Zetasizer and a quartz cuvette (ZEN2112, Malvern). Ten spectra measures were recorded for eleven replicates at 25 °C. The standard operating procedure accounted for 5% glycerol in solution. % volume was collected and reported. (SI 2.12) DLS Titration Experiment – 6 µM, 3 µM, 1.5 µM, 0.5 µM, 0.1 µM pyAtzA was phosphorylated (as described previously) with an incubation time of overnight at 25°C. Either AtzCM1 wildtype (WT) or AtzCM1 superbinder (SB) was added to each sample at 2 µM, 1 µM, 0.5 µM, 0.25 µM, 0.50 µM final concentration. The sample was allowed to incubate for 2 hr at 25°C. Therefore, the final concentrations of all components was from 3 µM – 0.05 µM pyAtzA, 2 µM – 0.05 µM AtzCM1-WT or AtzCM1-SB. DLS was performed at 25°C, 50 µL/sample volume, in a low-volume quartz sizing cuvette (Malvern; ZEN2112) using a Zetasizer Nano ZS (Malvern). Measurements were performed in duplicate with each sample read and averaged 15 times.<br>
DOI: 10.6084/m9.figshare.7956026.v1
title: Supplementary Figure 7 Phosphorylation of SH2 peptide AtzA fusion (pY-AtzA) by Src kinase

description: Article: Stimulus-responsive Self-Assembly of Protein-Based Fractals by Computational Design Pre-print: bioRxiv 274183; doi: https://doi.org/10.1101/274183 Figure: S7. Phosphorylation of SH2 peptide AtzA fusion (pY-AtzA) by Src kinase. In order to verify phosphorylation of AtzA by Src kinase into phosphorylated SH2 peptide AtzA fusion (pY-AtzA), ELISA with (1:4000 dilution) antiphosphotyrosine-horseradish peroxidase conjugate was performed on pY-AtzA samples either with Src kinase (+) or without Src kinase (-), in phosphorylation reaction buffer at 1.25 µg/mL pY-AtzA or 20 µg/mL pY-AtzA. Data is presented as mean ± 1 standard deviation. (SI 2.9) Phosphorylation, assembly formation, and disassembly – The phosphorylation protocol was based upon Src kinase activity assay by Sigma (Catalog # S1076). In a final reaction volume of 150μL, 3μM AtzAM1 was mixed into 1X Kinase Activity Buffer (4mM MgCl2, 2.5mM MnCl2, 0.25mM DTT, 5mM MOPS, 2.5mM glycerol-2-phosphate, 1mM EGTA, 400nM EDTA, pH 7.6), 2.5 mM MnCl2,HNG, 2 mM ATP, 800ng Src kinase, and incubated for 7 – 16 hr at 25°C for phosphorylation to occur. After phosphorylating, AtzCM1 was added to a final 2μM concentration. Assembly was allowed to form at 2hr 25°C. Disassembly was performed by adding 4.8μg of YopH phosphatase into the 150μL reaction mixture after assembly formation occurred. Size measurements using DLS were performed to determine assembly formation/disassembly. (SI 2.7) Enzyme-linked immunosorbent assay (ELISA) – Phosphorylated AtzAM1 (pY27 AtzAM1) was loaded onto clear flat-bottom immuno 96-well plates (Thermo Scientific item #442404) at 20μg/mL and 1.25μg/mL in 50μL 1X PBS (Gibco pH 7.4, #10010023) overnight at 4◦C. Plates were rinsed twice in 200μL 1X TBS (Biorad #1706435). 1% BSA in TBS 0.05% Tween 20 was used to block wells at 200μL block solution for 1.5hr at 25°C under gentle agitation. Anti-phosphotyrosine 4G10 Platinum HRP conjugate (EMD #16-316) was diluted 1:5000 in 1% BSA TBS 0.05% Tween 20 and loaded onto the well at 25°C for 1.5hr under gentle agitation. Excess anti-phosphotyrosine was washed off with 200μL of TBS 0.05% Tween 20 in triplicate. To detect bound antibody, 100μL of TMB substrate reagent (Biolegend #421101) was added to each well and incubated for 5 minutes at 25°C. 100μL of TMB stop solution (Biolegend #423001) was added to the wells. Absorbance was read at 450nm using the Tecan Infinite M200 Pro plate reader.****Note: This work was part of the <b>Rutgers Biomod 2016 </b>project (M. Liu, A. Permaul, O. Dineen, M. Khalid, M. Shea, G.L. Bilker). See reference for additional details.
DOI: 10.6084/m9.figshare.12878660.v1
title: Additional file 3 of Expression of microRNA and their gene targets are dysregulated in preinvasive breast cancer

description: Additional file 3: List of microRNA considered present or absent in each histological group. (XLS 210 KB)
DOI: 10.6084/m9.figshare.7955993
title: PEPX Logfile.xls

description: Full dataset of the PEPX Study
DOI: 10.6084/m9.figshare.7956032.v1
title: Supplementary Figure 19 Average size of particle formed by pY-AtzA and wild type AtzC-SH2

description: Article: Stimulus-responsive Self-Assembly of Protein-Based Fractals by Computational Design Pre-print: bioRxiv 274183; doi: https://doi.org/10.1101/274183 Figure: S19. Average size of particle formed by pY-AtzA and wild type AtzC-SH2. (A) Heat map showing volume-weighted mean size of particles found from 50-3000 nM pY-AtzA and 50-2000 nM AtzC-SH2. Value shown is average of two physical samples. Histogram illustrates distribution of sizes found on heatmap. (B) Volume distributions of heat map. Distributions shown are representative of other traces in the sample. (SI 2.9) Phosphorylation, assembly formation, and disassembly – The phosphorylation protocol was based upon Src kinase activity assay by Sigma (Catalog # S1076). In a final reaction volume of 150μL, 3μM AtzAM1 was mixed into 1X Kinase Activity Buffer (4mM MgCl2, 2.5mM MnCl2, 0.25mM DTT, 5mM MOPS, 2.5mM glycerol-2-phosphate, 1mM EGTA, 400nM EDTA, pH 7.6), 2.5 mM MnCl2,HNG, 2 mM ATP, 800ng Src kinase, and incubated for 7 – 16 hr at 25°C for phosphorylation to occur. After phosphorylating, AtzCM1 was added to a final 2μM concentration. Assembly was allowed to form at 2hr 25°C. Disassembly was performed by adding 4.8μg of YopH phosphatase into the 150μL reaction mixture after assembly formation occurred. Size measurements using DLS were performed to determine assembly formation/disassembly. (SI 2.10) Dynamic light scattering (DLS) – 50 μL of an assembly sample was used for size determination using a Malvern Zetasizer and a quartz cuvette (ZEN2112, Malvern). Ten spectra measures were recorded for eleven replicates at 25 °C. The standard operating procedure accounted for 5% glycerol in solution. % volume was collected and reported. (SI 2.12) DLS Titration Experiment – 6 µM, 3 µM, 1.5 µM, 0.5 µM, 0.1 µM pyAtzA was phosphorylated (as described previously) with an incubation time of overnight at 25°C. Either AtzCM1 wildtype (WT) or AtzCM1 superbinder (SB) was added to each sample at 2 µM, 1 µM, 0.5 µM, 0.25 µM, 0.50 µM final concentration. The sample was allowed to incubate for 2 hr at 25°C. Therefore, the final concentrations of all components was from 3 µM – 0.05 µM pyAtzA, 2 µM – 0.05 µM AtzCM1-WT or AtzCM1-SB. DLS was performed at 25°C, 50 µL/sample volume, in a low-volume quartz sizing cuvette (Malvern; ZEN2112) using a Zetasizer Nano ZS (Malvern). Measurements were performed in duplicate with each sample read and averaged 15 times.<br>
DOI: 10.6084/m9.figshare.12878660
title: Additional file 3 of Expression of microRNA and their gene targets are dysregulated in preinvasive breast cancer

description: Additional file 3: List of microRNA considered present or absent in each histological group. (XLS 210 KB)
DOI: 10.6084/m9.figshare.7955990
title: Genotyping MDR1.xls

description: Full dataset of MDR1 genotypes of participants of PEPX study
DOI: 10.6084/m9.figshare.7955972
title: Supplementary Figure 31 and 32 Helium ion microscopy (HIM) images depict fractal-like assembly with 3 µM AtzAM1, 1 µMAtzBSH2, 1 µM or 2 µM AtzCM1 final protein concentrations

description: Supp Figure 31: <b>Helium ion microscopy (HIM) images depict fractal-like assembly with 3 µM AtzAM1, 1 µMAtzBSH2, 1 µM AtzCM1 final protein concentrations.</b> (A to D) Various views of the fractal-like 3-component assembly are shown. Supp Figure 32: <b>Helium ion microscopy (HIM) images depict fractal-like assembly with 3 µM AtzAM1, 1 µMAtzBSH2, 2 µM AtzCM1 final concentrations.</b> (A to H) Various views of the 3-component assembly with fractal-like structures are shown.
DOI: 10.6084/m9.figshare.7955993.v1
title: PEPX Logfile.xls

description: Full dataset of the PEPX Study
DOI: 10.25392/leicester.data.7955969
title: Dual-target search: Datasets for Experiment 1 and 2

description: Data files contain summary data for participants in Experiments 1 and 2 reported in a submitted manuscript entitled, "Concurrent evaluation of independently cued features during perceptual decisions and saccadic targeting in visual search."<br>gDataExp1.xlsx: Proportion of correct responses. The experiment used a 2 (search type: single- vs. dual-target) x 2 (target-present vs. -absent) x 3 (set size: 1, 2 & 4) factorial design. Columns represent cells in the factorial design and headings contain the following notation:"sT" and "dT" = single- and dual-target searches"1", "2" and "4" are set sizes"H" and "CR" are hits and correct rejections. <br>gDataExp2.xlsx.Proportion of 1st fixations and saccadic latencies to targets and distractors during overt search. The experiment used a 2 (search type: single- vs. dual-target) x 3 (object: cued-target, similar distractor & dissimilar distractor) factorial design. Columns represent cells in the factorial design and headings contain the following notation:"T1" = cued-target"D1" = similar distractor"D2" = dissimilar distractor<br>
DOI: 10.6084/m9.figshare.7955972.v1
title: Supplementary Figure 31 and 32 Helium ion microscopy (HIM) images depict fractal-like assembly with 3 µM AtzAM1, 1 µMAtzBSH2, 1 µM or 2 µM AtzCM1 final protein concentrations

description: Supp Figure 31: <b>Helium ion microscopy (HIM) images depict fractal-like assembly with 3 µM AtzAM1, 1 µMAtzBSH2, 1 µM AtzCM1 final protein concentrations.</b> (A to D) Various views of the fractal-like 3-component assembly are shown. Supp Figure 32: <b>Helium ion microscopy (HIM) images depict fractal-like assembly with 3 µM AtzAM1, 1 µMAtzBSH2, 2 µM AtzCM1 final concentrations.</b> (A to H) Various views of the 3-component assembly with fractal-like structures are shown.
DOI: 10.6084/m9.figshare.7955990.v1
title: Genotyping MDR1.xls

description: Full dataset of MDR1 genotypes of participants of PEPX study
DOI: 10.6084/m9.figshare.7955960
title: Results and graphs of a questionnaire based survey on effects of metal detecting among British Armed Forces veterans with PTSD and/or other mental health challenges.

description: Sorted results and graphs of a questionnaire based survey on self-assessment of the effects of metal detecting among British Armed Forces veterans with PTSD (Post Traumatic Stress Disorder) and/or other diagnosed or undiagnosed psychological challenges.
DOI: 10.25392/leicester.data.7955969.v1
title: Dual-target search: Datasets for Experiment 1 and 2

description: Data files contain summary data for participants in Experiments 1 and 2 reported in a submitted manuscript entitled, "Concurrent evaluation of independently cued features during perceptual decisions and saccadic targeting in visual search."<br>gDataExp1.xlsx: Proportion of correct responses. The experiment used a 2 (search type: single- vs. dual-target) x 2 (target-present vs. -absent) x 3 (set size: 1, 2 & 4) factorial design. Columns represent cells in the factorial design and headings contain the following notation:"sT" and "dT" = single- and dual-target searches"1", "2" and "4" are set sizes"H" and "CR" are hits and correct rejections. <br>gDataExp2.xlsx.Proportion of 1st fixations and saccadic latencies to targets and distractors during overt search. The experiment used a 2 (search type: single- vs. dual-target) x 3 (object: cued-target, similar distractor & dissimilar distractor) factorial design. Columns represent cells in the factorial design and headings contain the following notation:"T1" = cued-target"D1" = similar distractor"D2" = dissimilar distractor<br>
DOI: 10.6084/m9.figshare.7955942
title: CCDB_3693.jpg

description: Z projection through a through-focus series of a medium spiny neuron from a dopamine transporter knock out mouse, iinjected with Lucifer Yellow and then photoconverted.
DOI: 10.6084/m9.figshare.7955954
title: Supplementary Figure 30 and 34 Fluorescence microscopy and bright-field images of the 4-component assembly confirm incorporation of IgG-Alexa Fluor 568 or AtzBSH2 into assembly

description: Supp Figure 30: <b>Fluorescence microscopy and bright-field images of the 4-component assembly</b> (AtzAM1, AtzCM1, ProteinA-SH2, and antibody, along with extended linker versions of AtzA and AtzC) <b>confirm incorporation of IgG-Alexa Fluor 568 into assemblies.</b> (A) Fractal assembly in DIC and (B) fluorescent image of fractal indicating incorporation of antibody into assembly. (C) Globular assembly in DIC and (D) fluorescent images of globular assembly indicating incorporation of antibody into assembly. The depiction of a fractal and globular topology is easily distinguishable in these images. Supp Figure 34: <b>Fluorescence microscopy and bright-field images of the 3-component assembly confirm incorporation of AtzBSH2 into assembly while bright-field images confirm the fractal-like nature of the 2-component assembly. </b>(A and B) 3 µM AtzAM1, 1 µMAtzBSH2 dye labeled with Alexa FluorTM 647, 2 µM AtzCM1 image shows AtzBSH2 incorporation into 3-component assembly at various locations (C to H) 3 µM AtzAM1 and 2 µM AtzCM1 assembly images depict fractal-like assembly structure.<br>
DOI: 10.6084/m9.figshare.7955957
title: CCDB_3696.jpg

description: Single computed slice through a tomographic reconstruction of a Node of Ranvier from rat peripheral nerve, prepared by a combination of chemical fixation, high pressure freezing and freeze substitution
DOI: 10.6084/m9.figshare.7955942.v1
title: CCDB_3693.jpg

description: Z projection through a through-focus series of a medium spiny neuron from a dopamine transporter knock out mouse, iinjected with Lucifer Yellow and then photoconverted.
DOI: 10.6084/m9.figshare.7955957.v1
title: CCDB_3696.jpg

description: Single computed slice through a tomographic reconstruction of a Node of Ranvier from rat peripheral nerve, prepared by a combination of chemical fixation, high pressure freezing and freeze substitution
DOI: 10.6084/m9.figshare.7955891
title: Squamata subset positive selection analyses

description: Data used for positive selection analyses across squamata species subset. Taxa include Anolis carolinensis, Varanus komodoensis, Python molurus bivitattus, and Gekko japonicus. This includes protein sequence alignments, coding sequence alignments, and the species tree.
DOI: 10.6084/m9.figshare.7955897
title: Supplementary Figure 25 Transmission Electron Microscopy (TEM) depicts fractal-like assemblies in the phosphorylated samples while the non-phosphorylated samples depict individual proteins

description: <b>Transmission Electron Microscopy (TEM) depicts fractal-like assemblies in the phosphorylated samples while the non-phosphorylated samples depict individual proteins.</b> (<b>A </b>and <b>B</b>) ten-fold dilution of 3 µM non-pY-AtzAM1 and 2 µM AtzCM1, which shows the individual proteins. (<b>C </b>to <b>F</b>) Various assembly images of the ten-fold dilution of 3 µM pY-AtzAM1 and 2 µM AtzCM1 sample which form the fractal-like assembly consistently. (<b>G</b>) Image analysis (2D) using box counting yields the expected fractal dimension of ~1.7 for the C, D, and E, TEM images.
DOI: 10.6084/m9.figshare.7955960.v1
title: Results of a questionnaire based survey on effects of metal detecting among British Armed Forces veterans with PTSD and/or other mental health challenges.

description: Sorted and coded results of a questionnaire based survey on self-assessment of the effects of metal detecting among British Armed Forces veterans with PTSD (Post Traumatic Stress Disorder) and/or other diagnosed or undiagnosed psychological challenges.
DOI: 10.6084/m9.figshare.7955885
title: Supplementary Figure 24 Helium ion microscopy comparison of fractal assembly and globular assembly

description: <b>Helium ion microscopy comparison of fractal assembly and globular assembly.</b> HIM Images depict fractal-like assembly with 3 uM AtzAM1 and 2 uM AtzCM1 final concentrations (<b>A </b>to <b>D</b>), while the 3 uM AtzAM1-ExtendedLinker and 2 uM AtzCM1-ExtendedLinker final concentrations show both large and small globular shape proteins on the silicon surface (<b>E</b> to <b>H</b>).
DOI: 10.6084/m9.figshare.7955897.v1
title: Supplementary Figure 25 Transmission Electron Microscopy (TEM) depicts fractal-like assemblies in the phosphorylated samples while the non-phosphorylated samples depict individual proteins

description: <b>Transmission Electron Microscopy (TEM) depicts fractal-like assemblies in the phosphorylated samples while the non-phosphorylated samples depict individual proteins.</b> (<b>A </b>and <b>B</b>) ten-fold dilution of 3 µM non-pY-AtzAM1 and 2 µM AtzCM1, which shows the individual proteins. (<b>C </b>to <b>F</b>) Various assembly images of the ten-fold dilution of 3 µM pY-AtzAM1 and 2 µM AtzCM1 sample which form the fractal-like assembly consistently. (<b>G</b>) Image analysis (2D) using box counting yields the expected fractal dimension of ~1.7 for the C, D, and E, TEM images.
DOI: 10.6084/m9.figshare.7955879
title: All squamata positive selection analyses

description: Protein alignments, coding sequence alignments, and reference species tree used for detecting positive selection in the Komodo dragon.