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image processing cryo em data  (JEOL)
93
JEOL image processing cryo em data
Image Processing Cryo Em Data, supplied by JEOL, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/JEM-3300+Transmission+Electron+Microscope/pm41170989-180-4-17
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s2 cryo em image processing  (Thermo Fisher)
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Thermo Fisher s2 cryo em image processing
( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) <t>Cryo-EM</t> structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. <t>S2</t> . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .
S2 Cryo Em Image Processing, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/SUCROSE+EP%2FBP%2FNF+12KG/bio_rxiv__2023__12__17__572070-278-20-21
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s2 cryo em image processing - by Bioz Stars, 2026-09
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cryo-em data collection and image processing  (NanoImaging Services Inc)
90
NanoImaging Services Inc cryo-em data collection and image processing
( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) <t>Cryo-EM</t> structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. <t>S2</t> . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .
Cryo Em Data Collection And Image Processing, supplied by NanoImaging Services Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/cryo+em+data+collection+and+image+processing/pm40340250-304-4-10
Average 90 stars, based on 1 article reviews
cryo-em data collection and image processing - by Bioz Stars, 2026-09
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cryo-em image-processing pipeline  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc cryo-em image-processing pipeline
( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) <t>Cryo-EM</t> structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. <t>S2</t> . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .
Cryo Em Image Processing Pipeline, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/cryo+em+image+processing+pipeline/pm38838667-864-39-46
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cryo-em image-processing pipeline - by Bioz Stars, 2026-09
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cryo em image processing  (Thermo Fisher)
99
Thermo Fisher cryo em image processing
( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) <t>Cryo-EM</t> structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. <t>S2</t> . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .
Cryo Em Image Processing, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/SUCROSE+EP%2FBP%2FNF+12KG/pm37587688-75-3-3
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cryo em image processing - by Bioz Stars, 2026-09
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image processing cryo em data acquisition  (JEOL)
93
JEOL image processing cryo em data acquisition
( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) <t>Cryo-EM</t> structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. <t>S2</t> . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .
Image Processing Cryo Em Data Acquisition, supplied by JEOL, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/JEM-3300+Transmission+Electron+Microscope/pm37626059-228-4-18
Average 93 stars, based on 1 article reviews
image processing cryo em data acquisition - by Bioz Stars, 2026-09
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cryo-em image processing pipeline  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc cryo-em image processing pipeline
( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) <t>Cryo-EM</t> structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. <t>S2</t> . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .
Cryo Em Image Processing Pipeline, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cryo+em+image+processing/cryo+em+image+processing+pipeline/pmc10197580__NIHPP2023__05__08__539880v1___supplement___1-25-0-6
Average 90 stars, based on 1 article reviews
cryo-em image processing pipeline - by Bioz Stars, 2026-09
90/100 stars
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Image Search Results


( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) Cryo-EM structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. S2 . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .

Journal: bioRxiv

Article Title: Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome

doi: 10.1101/2023.12.17.572070

Figure Lengend Snippet: ( A ) Co-immunoprecipitation assays to test self-association of NRC2 and ZAR1 from N. benthamiana . C-terminally 3xFLAG-tagged NbNRC2 and NbZAR1 proteins were coexpressed with C-terminally 4xMyc tagged NbNRC2 or NbZAR1. Immunoprecipitations were performed with agarose beads conjugated to FLAG antibodies (FLAG IP). Total protein extracts were immunoblotted with the antisera labelled on the left. Approximate molecular weights (in kDa) of the proteins are shown on the right. Protein loading control was carried out using Ponceau stain (PS). The experiment was performed three times with similar results. ( B ) 2D classifications from negative staining transmission electron microscopy images of affinity-purified NbNRC2. NRC2 appears as a dimer, with a maximum dimension of approximately 150 Å at its widest point. Scale bar = 230 Å. ( C ) Cryo-EM structure of resting state of NRC2 dimers. Atomic model corresponding to NRC2 homodimer shown in two orthogonal views, with resolved NB domain (NBD), HD1-WHD and LRR domains. Notably, the N-terminal CC domain of NRC2 was absent from the Cryo-EM density. Inset shows details of interfaces between the two NRC2 protomers, highlighting amino acid stretches corresponding to three contact interfaces. ( D ) Color coding of the domains is shown in the schematic representation of the domain architecture and boundaries of NRC2, which includes the exact boundaries of the amino acid stretches at the dimerization interfaces. A schematic representation of the pipeline used for Cryo-EM imaging, data processing and model building can be found in Fig. S2 . Additional views of the structure and dimerization interface can be found in Fig. S3, Fig. S4 and Movie S1 . Additional information on image processing and model building can be found in Table S1 .

Article Snippet: Approximate molecular weights (kDa) of the proteins are shown on the left of the green panel. biorxiv;2023.12.17.572070v1/FIGS2 F7 figs2 Fig. S2: Cryo-EM image processing and 3D-reconstruction of NRC2 homodimers.

Techniques: Immunoprecipitation, Staining, Negative Staining, Transmission Assay, Electron Microscopy, Affinity Purification, Cryo-EM Sample Prep, Imaging

Journal: bioRxiv

Article Title: Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome

doi: 10.1101/2023.12.17.572070

Figure Lengend Snippet:

Article Snippet: Approximate molecular weights (kDa) of the proteins are shown on the left of the green panel. biorxiv;2023.12.17.572070v1/FIGS2 F7 figs2 Fig. S2: Cryo-EM image processing and 3D-reconstruction of NRC2 homodimers.

Techniques: