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Easiglow glow discharge cleaning system

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The EasiGlow Glow Discharge Cleaning System is a laboratory equipment designed for cleaning and activating the surface of various materials. It uses a glow discharge process to remove contaminants and modify the surface properties of the sample.

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Lab products found in correlation

K3 detector, by Ametek (6 mentions) Leica em gp2 plunge freezer, by Leica Microsystems (6 mentions) Titan krios, by Thermo Fisher Scientific (6 mentions) Lacey carbon grid, by Electron Microscopy Sciences (1 mentions) Talos 120c, by Thermo Fisher Scientific (1 mentions)

7 protocols using easiglow glow discharge cleaning system

1

Cryo-EM structure determination of SARS-CoV-2 spike

Cited 1 time
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Purified SARS-CoV-2 spike ectodomains were diluted to a concentration of ~1.5 mg/ml in 2 mM Tris pH 8.0, 200 mM NaCl and 0.02% NaN3 and 0.5% glycerol was added. A 2.3-μl drop of protein was deposited on a Quantifoil-1.2/1.3 grid (Electron Microscopy Sciences) that had been glow-discharged for 10 s using a PELCO easiGlow Glow Discharge Cleaning System. After a 30-s incubation in >95% humidity, excess protein was blotted away for 2.5 s before being plunge-frozen into liquid ethane using a Leica EM GP2 plunge freezer (Leica Microsystems). Frozen grids were imaged using a Titan Krios (Thermo Fisher) equipped with a K3 detector (Gatan). CryoSPARC (58 (link)) software was used for data processing. Phenix (54 (link), 59 (link)), Coot (60 (link)), Pymol (61 ), Chimera (62 (link)), ChimeraX (63 (link)), and Isolde (64 (link)) were used for model building and refinement.
Gobeil S.M., Janowska K., McDowell S., Mansouri K., Parks R., Stalls V., Kopp M.F., Manne K., Li D., Wiehe K., Saunders K.O., Edwards R.J., Korber B., Haynes B.F., Henderson R, & Acharya P. (2021). Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity. Science (New York, N.y.), 373(6555), eabi6226.
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2

Cryo-EM Structure Determination of SARS-CoV-2 Spike

Cited 1 time
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Purified SARS-CoV-2 spike ectodomains were diluted to a concentration of ∼1.5 mg/mL in 2 mM Tris pH 8.0, 200 mM NaCl and 0.02% NaN3 and 0.5% glycerol was added. A 2.3-μL drop of protein was deposited on a Quantifoil-1.2/1.3 grid (Electron Microscopy Sciences, PA) that had been glow discharged for 10 s using a PELCO easiGlow Glow Discharge Cleaning System. After a 30 s incubation in >95% humidity, excess protein was blotted away for 2.5 s before being plunge frozen into liquid ethane using a Leica EM GP2 plunge freezer (Leica Microsystems). Frozen grids were imaged using a Titan Krios (Thermo Fisher) equipped with a K3 detector (Gatan). The cryoSPARC (Punjani et al., 2017 (link)) software was used for data processing. Phenix (Liebschner et al., 2019 (link); Afonine et al., 2018 (link)), Coot (Emsley et al., 2010 (link)), Pymol (Schrodinger, 2015 ), Chimera (Pettersen et al., 2004 (link)), ChimeraX (Goddard et al., 2018 (link)) and Isolde (Croll, 2018 (link)) were used for model building and refinement.
Stalls V., Lindenberger J., Gobeil S.M., Henderson R., Parks R., Barr M., Deyton M., Martin M., Janowska K., Huang X., May A., Speakman M., Beaudoin E., Kraft B., Lu X., Edwards R.J., Eaton A., Montefiori D.C., Williams W.B., Saunders K.O., Wiehe K., Haynes B.F, & Acharya P. (2022). Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike. Cell Reports, 39(13), 111009.
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3

SARS-CoV-2 Spike Protein Structure Determination

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Purified SARS-CoV-2 S protein ectodomains were diluted to a concentration of ∼1.5 mg/mL in 2 mM Tris pH 8.0, 200 mM NaCl and 0.02% NaN3 and 0.5% glycerol was added. A 2.3-μL drop of protein was deposited on a Quantifoil-1.2/1.3 grid (Electron Microscopy Sciences, PA) that had been glow discharged for 10 seconds using a PELCO easiGlow™ Glow Discharge Cleaning System. After a 30-second incubation in >95% humidity, excess sample was blotted away from the grid for 2.5 seconds using a Whatman 1 filter paper before being plunged into liquid ethane using a Leica EM GP2 plunge freezer (Leica Microsystems). Frozen grids were imaged using a Titan Krios (Thermo Fisher) equipped with a K3 detector (Gatan). The cryoSPARC (Punjani et al., 2017 (link)) software was used for data processing. Phenix (Liebschner et al., 2019 (link), Afonine et al., 2018 (link)), Coot (Emsley et al., 2010 (link)), Pymol (Schrödinger, 2015 ), Chimera (Pettersen et al., 2004 (link)), ChimeraX (Goddard et al., 2018 (link)) and Isolde (Croll, 2018 (link)) were used for model building and refinement.
Gobeil S.M., Henderson R., Stalls V., Janowska K., Huang X., May A., Speakman M., Beaudoin E., Manne K., Li D., Parks R., Barr M., Deyton M., Martin M., Mansouri K., Edwards R.J., Eaton A., Montefiori D.C., Sempowski G.D., Saunders K.O., Wiehe K., Williams W., Korber B., Haynes B.F, & Acharya P. (2022). Structural diversity of the SARS-CoV-2 Omicron spike. Molecular Cell, 82(11), 2050-2068.e6.
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4

Negative Staining for EM Protein Analysis

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For EM analysis of negatively stained samples, 4 µL of protein (diluted to about 100 nM concentration) was applied to lacey carbon grids (Electron Microscopy Sciences) pretreated with a PELCO easiGlow Glow Discharge Cleaning System (15 mA, 15-s, negative polarity). The solution was blotted by filter paper from the side after 1 min. Two droplets (10 µL each) of 2% uranyl acetate were then consecutively applied to the grid surface and each blotted after 10 s. A third droplet of uranyl acetate was then applied and blotted after 60 s, and then, the grid was dried before loading onto a Talos 120C (Thermo Fisher, housed in the Johns Hopkins MicFac) for imaging at 120 keV.
Liu C., Hauk G., Yan Q, & Berger J.M. (2024). Structure of Escherichia coli exonuclease VII. Proceedings of the National Academy of Sciences of the United States of America, 121(5), e2319644121.
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5

Cryo-EM Structure Determination of SARS-CoV-2 Spike

Cited 1 time
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Purified SARS-CoV-2 spike ectodomains were diluted to a concentration of ~1.5 mg/mL in 2 mM Tris pH 8.0, 200 mM NaCl and 0.02% NaN3 and 0.5% glycerol was added. A 2.3-μL drop of protein was deposited on a Quantifoil-1.2/1.3 grid (Electron Microscopy Sciences, PA) that had been glow discharged for 10 seconds using a PELCO easiGlow™ Glow Discharge Cleaning System. After a 30-second incubation in >95% humidity, excess protein was blotted away for 2.5 seconds before being plunge frozen into liquid ethane using a Leica EM GP2 plunge freezer (Leica Microsystems). Frozen grids were imaged using a Titan Krios (Thermo Fisher) equipped with a K3 detector (Gatan). The cryoSPARC (59 (link)) software was used for data processing. Phenix (54 (link), 60 (link)), Coot (61 (link)), Pymol (62 ), Chimera (63 (link)), ChimeraX (64 (link)) and Isolde (65 (link)) were used for model building and refinement.
Gobeil S.M., Janowska K., McDowell S., Mansouri K., Parks R., Stalls V., Kopp M.F., Manne K., Li D., Wiehe K., Saunders K.O., Edwards R.J., Korber B., Haynes B.F., Henderson R, & Acharya P. (2021). Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity. Science (New York, N.y.), 373(6555), eabi6226.
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6

Structural Analysis of SARS-CoV-1 Spike Protein

Cited 1 time
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Purified SARS-CoV-1 spike ectodomain was incubated for approximatively 2 hours with a 6-fold molar equivalent of the DH1047 Fab in a final volume of 10μL. The sample concentration was adjusted to ~1.5 mg/mL of spike in 2 mM Tris pH 8.0, 200 mM NaCl, and 0.02% NaN3. Before freezing, 0.1μL of glycerol was added to the 10μL of sample. A 2.4-μL drop of protein was deposited on a Quantifoil-1.2/1.3 grid (Electron Microscopy Sciences, PA) that had been glow discharged for 10 seconds using a PELCO easiGlow™ Glow Discharge Cleaning System. After a 30-second incubation in >95% humidity, excess protein was blotted away for 2.5 seconds before being plunge frozen into liquid ethane using a Leica EM GP2 plunge freezer (Leica Microsystems). Frozen grids were imaged using a Titan Krios (Thermo Fisher) equipped with a K3 detector (Gatan). Data processing was performed using cryoSPARC39 (link). Model building and refinement was done using Phenix40 (link),41 (link), Coot42 (link), Pymol43 , Chimera44 (link), ChimeraX45 (link) and Isolde46 (link).
Martinez D.R., Schaefer A., Gobeil S., Li D., De la Cruz G., Parks R., Lu X., Barr M., Manne K., Mansouri K., Edwards R.J., Yount B., Anasti K., Montgomery S.A., Shen S., Zhou T., Kwong P.D., Graham B.S., Mascola J.R., Montefiori D.C., Alam M., Sempowski G.D., Wiehe K., Saunders K.O., Acharya P., Haynes B.F, & Baric R.S. (2021). A broadly neutralizing antibody protects against SARS-CoV, pre-emergent bat CoVs, and SARS-CoV-2 variants in mice. bioRxiv.
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7

Cryo-EM Structure of SARS-CoV-2 Spike Ectodomain

Cited 1 time
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Purified SARS-CoV-2 spike ectodomains were diluted to a concentration of ~ 1.5 mg/mL in 2 mM Tris pH 8.0, 200 mM NaCl and 0.02% NaN3 and 0.5% glycerol was added. A 2.4-μL drop of protein was deposited on a Quantifoil-1.2/1.3 grid (Electron Microscopy Sciences, PA) that had been glow discharged for 10 s using a PELCO easiGlow Glow Discharge Cleaning System. After a 30 s incubation in >95% humidity, excess protein was blotted away for 2.5 s before being plunge frozen into liquid ethane using a Leica EM GP2 plunge freezer (Leica Microsystems). Frozen grids were imaged using a Titan Krios (Thermo Fisher) equipped with a K3 detector (Gatan). The cryoSPARC (53 (link)) software was used for data processing. Phenix (54 (link), 55 (link)), Coot (56 (link)), Pymol (57 ), Chimera (58 (link)), ChimeraX (59 (link)) and Isolde (60 (link)) were used for model building and refinement.
Malewana R.D., Stalls V., May A., Lu X., Martinez D.R., Schäfer A., Li D., Barr M., Sutherland L.L., Lee E., Parks R., Beck W.E., Newman A., Bock K.W., Minai M., Nagata B.M., DeMarco C.T., Denny T.N., Oguin TH I.I.I., Rountree W., Wang Y., Mansouri K., Edwards R.J., Sempowski G.D., Eaton A., Muramatsu H., Henderson R., Tam Y., Barbosa C., Tang J., Cain D.W., Santra S., Moore I.N., Andersen H., Lewis M.G., Golding H., Seder R., Khurana S., Montefiori D.C., Pardi N., Weissman D., Baric R.S., Acharya P., Haynes B.F, & Saunders K.O. (2023). Broadly neutralizing antibody induction by non-stabilized SARS-CoV-2 Spike mRNA vaccination in nonhuman primates. bioRxiv.
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