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talos n  (Bruker Corporation)


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    Bruker Corporation talos n
    Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
    Talos N, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 99/100, based on 14296 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail."

    Article Title: The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail.

    Journal: Structure (London, England : 1993)

    doi: 10.1016/j.str.2024.10.031

    Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) The TALOS-N secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
    Figure Legend Snippet: Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) The TALOS-N secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.

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    Article Title: The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail.
    Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER In vitro acetyltransferase assay: H4 experiment 1, control, raw data This study PRIDE: PXD052922 In vitro acetyltransferase assay: H4 experiment 1, KKT23, RNAi raw data This study PRIDE: PXD052922 In vitro acetyltransferase assay: H4 experiment 2, control, raw data This study PRIDE: PXD052922 In vitro acetyltransferase assay: H4 experiment 2, KKT23 RNAi, raw data This study PRIDE: PXD052922 In vitro acetyltransferase assay: H4 experiment 3, control, raw data This study PRIDE: PXD052922 In vitro acetyltransferase assay: H4 experiment 3, KKT23 RNAi, raw data This study PRIDE: PXD052922 IP-MS: GFP-KKT232 150 (KKT23N), raw data This study PRIDE: PXD052922 IP-MS: H2B-GFP experiment 1, control, raw data This study PRIDE: PXD052922 IP-MS: H2B-GFP experiment 1, KKT23 RNAi, raw data This study PRIDE: PXD052922 IP-MS: H2B-GFP experiment 2, control, raw data This study PRIDE: PXD052922 IP-MS: H2B-GFP experiment 2, KKT23 RNAi, raw data This study PRIDE: PXD052922 IP-MS: H2B-GFP experiment 3, control, raw data This study PRIDE: PXD052922 IP-MS: H2B-GFP experiment 3, KKT23 RNAi, raw data This study PRIDE: PXD052922 KKT23125 348 + acetyl-CoA chemical shifts This study BMRB: 52461 Trypanosoma brucei KKT232 70 crystal structure This study PDB: 9EVR Trypanosoma brucei native KKT23125 348 crystal structure This study PDB: 9EVQ Trypanosoma brucei selenomethionine KKT23125 348 crystal structure This study PDB: 9F5Q Experimental models: cell lines T. brucei: H2B-GFP, BAP249 This study N/A T. brucei: H2B-GFP, KKT23 RNAi, BAP2596 This study N/A T. brucei: tdTomato-KKT1, BAP171 This study N/A T. brucei: tdTomato-KKT1, GFP-NLS-KKT232 150 (KKT23N), BAP2296 This study N/A T. brucei: LacO at rDNA, BAP347 (Ishii and Akiyoshi)42 N/A T. brucei: LacO, TY-tdTomato-KKT22, BAP2158 This study N/A T. brucei: LacO, TY-tdTomato-KKT22, GFP-NLS-KKT232 150 (KKT23N)-LacI, BAP2547 This study N/A T. brucei: LacO, TY-tdTomato-KKT22, GFP-NLS-KKT23121 348 (KKT23C)-LacI, BAP2546 This study N/A T. brucei: KKT3-YFP, BAP1639 (Marcianò et al.)9 N/A T. brucei: KKT3-YFP, KKT23 RNAi, BAP2021 (Marcianò et al.)9 N/A Experimental models: organisms/strains Spodoptera frugiperda: Sf9 Thermo Fisher 12659017 Trypanosoma brucei brucei TREU 927/4 procyclic cells expressing T7 RNA polymerase and the tetracycline repressor to allow inducible expression (Poon et al.)43 SmOxP9 (Continued on next page) e3 Structure 33, 1–13.e1–e10, January 2, 2025 .. REAGENT or RESOURCE SOURCE IDENTIFIER ASTRA Wyatt Technology https://store.wyatt.com/shop/ viscostar/viscostar-iii/astra-software/ BUCCANEER (Cowtan et al.)49 http://www.ccp4.ac.uk/ CCPNmr (Vranken et al.)50 https://www.ccpn.ac.uk COOT (Emsley et al.)51 http://www2.mrc-lmb.cam.ac.uk/ Personal/pemsley/coot/ CRANK2 (Skubak et al.)52 http://www.ccp4.ac.uk/ DALI server (Holm)19 http://ekhidna2.biocenter.helsinki.fi/dali/ Diffraction Anisotropy Server (Strong et al.)53 http://services.mbi.ucla.edu/anisoscale/ DisEMBL (Linding et al.)54 http://dis.embl.de Foldseek (van Kempen et al.)20 https://github.com/steineggerlab/foldseek HMMER web server (Potter et al.)55 https://www.ebi.ac.uk/Tools/hmmer/ ImageJ (Schneider et al.)56 https://imagej.net Jalview (Waterhouse et al.)57 http://www.jalview.org/ MAFFT (Katoh et al.)58 https://mafft.cbrc.jp/alignment/server/ MaxQuant (Cox and Mann)59 https://www.maxquant.org/ NMRPipe (Delaglio et al.)60 https://spin.niddk.nih.gov/NMRPipe/ PHASER (McCoy et al.)61 http://www.ccp4.ac.uk/ PHENIX (Liebschner et al.)62 http://www.phenix-online.org/ pLink2 (Chen et al.)63 https://www.cog-genomics.org/plink/2.0/ PRIDE database (Perez-Riverol et al.)64 http://www.proteomexchange.org PyMOL (DeLano et al.)14 http://www.pymol.org/ SEDFIT (Schuck et al.)65 https://sedfitsedphat.github.io/ SEDNTERP (Hayes)66 http://www.jphilo.mailway.com/index.htm TALOS-N (Shen et al.)17 https://spin.niddk.nih.gov/bax/ software/TALOS-N/ TOPSPIN 3.2 Bruker Biospin https://www.bruker.com/service/ support-upgrades/softwaredownloads/nmr.html TriTryp database (Aslett et al.)67 https://tritrypdb.org UniProt (UniProt)68 https://www.uniprot.org xiView (Graham et al.)69 https://xiview.org/index.php .. REAGENT or RESOURCE SOURCE IDENTIFIER ASTRA Wyatt Technology https://store.wyatt.com/shop/ viscostar/viscostar-iii/astra-software/ BUCCANEER (Cowtan et al.)49 http://www.ccp4.ac.uk/ CCPNmr (Vranken et al.)50 https://www.ccpn.ac.uk COOT (Emsley et al.)51 http://www2.mrc-lmb.cam.ac.uk/ Personal/pemsley/coot/ CRANK2 (Skubak et al.)52 http://www.ccp4.ac.uk/ DALI server (Holm)19 http://ekhidna2.biocenter.helsinki.fi/dali/ Diffraction Anisotropy Server (Strong et al.)53 http://services.mbi.ucla.edu/anisoscale/ DisEMBL (Linding et al.)54 http://dis.embl.de Foldseek (van Kempen et al.)20 https://github.com/steineggerlab/foldseek HMMER web server (Potter et al.)55 https://www.ebi.ac.uk/Tools/hmmer/ ImageJ (Schneider et al.)56 https://imagej.net Jalview (Waterhouse et al.)57 http://www.jalview.org/ MAFFT (Katoh et al.)58 https://mafft.cbrc.jp/alignment/server/ MaxQuant (Cox and Mann)59 https://www.maxquant.org/ NMRPipe (Delaglio et al.)60 https://spin.niddk.nih.gov/NMRPipe/ PHASER (McCoy et al.)61 http://www.ccp4.ac.uk/ PHENIX (Liebschner et al.)62 http://www.phenix-online.org/ pLink2 (Chen et al.)63 https://www.cog-genomics.org/plink/2.0/ PRIDE database (Perez-Riverol et al.)64 http://www.proteomexchange.org PyMOL (DeLano et al.)14 http://www.pymol.org/ SEDFIT (Schuck et al.)65 https://sedfitsedphat.github.io/ SEDNTERP (Hayes)66 http://www.jphilo.mailway.com/index.htm TALOS-N (Shen et al.)17 https://spin.niddk.nih.gov/bax/ software/TALOS-N/ TOPSPIN 3.2 Bruker Biospin https://www.bruker.com/service/ support-upgrades/softwaredownloads/nmr.html TriTryp database (Aslett et al.)67 https://tritrypdb.org UniProt (UniProt)68 https://www.uniprot.org xiView (Graham et al.)69 https://xiview.org/index.php



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    Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
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    Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) The TALOS-N secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.

    Journal: Structure (London, England : 1993)

    Article Title: The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail.

    doi: 10.1016/j.str.2024.10.031

    Figure Lengend Snippet: Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) The TALOS-N secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.

    Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER ASTRA Wyatt Technology https://store.wyatt.com/shop/ viscostar/viscostar-iii/astra-software/ BUCCANEER (Cowtan et al.)49 http://www.ccp4.ac.uk/ CCPNmr (Vranken et al.)50 https://www.ccpn.ac.uk COOT (Emsley et al.)51 http://www2.mrc-lmb.cam.ac.uk/ Personal/pemsley/coot/ CRANK2 (Skubak et al.)52 http://www.ccp4.ac.uk/ DALI server (Holm)19 http://ekhidna2.biocenter.helsinki.fi/dali/ Diffraction Anisotropy Server (Strong et al.)53 http://services.mbi.ucla.edu/anisoscale/ DisEMBL (Linding et al.)54 http://dis.embl.de Foldseek (van Kempen et al.)20 https://github.com/steineggerlab/foldseek HMMER web server (Potter et al.)55 https://www.ebi.ac.uk/Tools/hmmer/ ImageJ (Schneider et al.)56 https://imagej.net Jalview (Waterhouse et al.)57 http://www.jalview.org/ MAFFT (Katoh et al.)58 https://mafft.cbrc.jp/alignment/server/ MaxQuant (Cox and Mann)59 https://www.maxquant.org/ NMRPipe (Delaglio et al.)60 https://spin.niddk.nih.gov/NMRPipe/ PHASER (McCoy et al.)61 http://www.ccp4.ac.uk/ PHENIX (Liebschner et al.)62 http://www.phenix-online.org/ pLink2 (Chen et al.)63 https://www.cog-genomics.org/plink/2.0/ PRIDE database (Perez-Riverol et al.)64 http://www.proteomexchange.org PyMOL (DeLano et al.)14 http://www.pymol.org/ SEDFIT (Schuck et al.)65 https://sedfitsedphat.github.io/ SEDNTERP (Hayes)66 http://www.jphilo.mailway.com/index.htm TALOS-N (Shen et al.)17 https://spin.niddk.nih.gov/bax/ software/TALOS-N/ TOPSPIN 3.2 Bruker Biospin https://www.bruker.com/service/ support-upgrades/softwaredownloads/nmr.html TriTryp database (Aslett et al.)67 https://tritrypdb.org UniProt (UniProt)68 https://www.uniprot.org xiView (Graham et al.)69 https://xiview.org/index.php

    Techniques: Sequencing