Solarus plasma cleaner

Manufactured by Ametek

Sourced in United States

The Solarus plasma cleaner is a laboratory equipment used for surface cleaning and treatment. It utilizes the power of plasma to remove organic contaminants and prepare surfaces for various applications. The core function of the Solarus plasma cleaner is to provide a controlled and effective cleaning process for samples or substrates.

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Lab products found in correlation

60 protocols using solarus plasma cleaner

Sar1-Coated TEM Grid Preparation

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Sar1-coated tubes were prepared as described above. Carbon-coated copper grids were glow-discharged for 8-10 seconds using a Gatan Solarus plasma cleaner (Gatan, Pleasanton, CA). The samples were adsorbed onto the grids for 1-2 minutes, washed with MSB, then stained with 2% uranyl acetate for 1-2 minutes and allowed to air dry before visualization using transmission electron microscopy (TEM).

Hariri H., Bhattacharya N., Johnson K., Noble A.J, & Stagg S.M. (2014). Insights into the Mechanisms of Membrane Curvature and Vesicle Scission by the Small GTPase Sar1 in the Early Secretory Pathway. Journal of molecular biology, 426(22), 3811-3826.

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Structural Analysis of Purified eIF3 Complexes

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Purified eIF3 complexes: WT (FLAG-eIF3e), Δ3h (FLAG-eIF3d), Δ3h (FLAG-eIF3f), and Δ3h (FLAG-eIF3m); (see Table 1) were diluted to ~50 nM in Tris-buffered saline (TBS) with 5% glycerol. Sample aliquots of 4 μl were pipetted onto 400 mesh continuous carbon grids, plasma cleaned in air for 10 s in a Solarus plasma cleaner (Gatan), and negatively stained with a 2% uranyl acetate solution. Data were acquired using a Philips CM200F electron microscope operating at 200 keV equipped with an UltraScan 1000 (Gatan) at a nominal magnification of 38,000× (2.8 Å/pixel). 2D data processing was carried out using the Relion and EMAN1.9 software packages (Ludtke et al., 1999 (link); Scheres, 2012 (link)). Particles were picked manually within Relion, with a box size of 120 × 120 pixels. The contrast transfer function (CTF) was estimated using CTFFind4 (Rohou and Grigorieff, 2015 (link)). Reference-free 2D classification was performed with CTFs ignored until the first peak for 25 rounds. Selected class averages were subsequently aligned and difference maps were created within EMAN1.9.

Smith M.D., Arake-Tacca L., Nitido A., Montabana E., Park A, & Cate J.H. (2016). Assembly of eIF3 Mediated by Mutually Dependent Subunit Insertion. Structure (London, England : 1993), 24(6), 886-896.

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Ebp1-Ribosome Complex Cryo-EM Prep

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Two batches of EM grids were prepared. The first batch used for collection of dataset 1 contained the in vivo pulled-out Ebp1–ribosome complex without addition of recombinant Ebp1. The second batch used for collection of dataset 2 contained the same purified ribosomes, but supplemented with recombinant Ebp1 (p48 isoform) to increase Ebp1 occupancy on the ribosomes. Right before freezing, Quantifoil Multi A holey carbon supported grids (Quantifoil, Multi A, 400 mesh) were glow-discharged for 10 s in oxygen atmosphere using a Solarus plasma cleaner (Gatan, Inc.). In total, 3 μL of freshly prepared samples (100 nM ribosomes without/with a eightfold excess of recombinant Ebp1) were directly applied to glow-discharged grids. Under a blot force of 0 at 100% humidity, the grids were blotted for 3 s with Whatman #1 filter papers using a Vitrobot Mark IV (FEI Company) operated at room temperature, and then immediately plunge-frozen in liquid ethane cooled with liquid nitrogen.

Wild K., Aleksić M., Lapouge K., Juaire K.D., Flemming D., Pfeffer S, & Sinning I. (2020). MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments. Nature Communications, 11, 776.

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Cryo-EM of ALB1 Nucleosome-FoxA1 Complex

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Aliquots (2.5 µl) of the purified ALB1 nucleosome mixed with the human FoxA1 deletion mutant, FoxA1(170–472), which contains both the DNA-binding and histone-binding domains, were applied to Quantifoil holey carbon grids (R1.2/1.3 200-mesh Cu), which were freshly cleaned using a Solarus Plasma Cleaner (Gatan, Pleasanton, USA) for 15 s at 20 W in a 23% H₂, 77% O₂ gas mix. The grids were blotted for 3 s at 16°C and 100% relative humidity, and then immediate plunge-frozen in liquid ethane with a Vitrobot Mark IV (Thermo Fisher, Hillsboro, USA). Cryo-EM data were collected using the EPU automation software on a Talos Arctica microscope (Thermo Fisher, Hillsboro, USA), operating at 200 kV at a calibrated magnification of 100 000× (pixel size of 1.40 Å), with defocus ranging from −1.5 to −3.0 µm. Digital micrographs were recorded with 2-second exposure times on a Falcon 3 direct electron detector (Thermo Fisher, Hillsboro, USA) in the linear mode, at a dose rate of approximately 40 electrons per Å² per second with 25 ms per frame time, retaining a total of 79 frames with an accumulated total dose of approximately 80 electrons per Å².

Takizawa Y., Tanaka H., Machida S., Koyama M., Maehara K., Ohkawa Y., Wade P.A., Wolf M, & Kurumizaka H. (2018). Cryo-EM structure of the nucleosome containing the ALB1 enhancer DNA sequence. Open Biology, 8(3), 170255.

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Structural Characterization of KcsA-Fab4 Complex

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Protein was expressed and purified using standard protocols. In brief, pET28a-KcsA [38 (link)] was expressed in E. coli DE3 pLysS (Novagen Millipore), and purified in HEPES, KCl and DDM by cobalt metal affinity chromatography and size exclusion chromatography (SEC). Purified Fab4 elbow variant were added in excess to purified KcsA, and the stoichiometric complex was further purified on SEC. The peak corresponding to the complex was collected, and used directly for grid preparation without further concentration.
C-flat 1.2/1.3, 200 Mesh cryoEM grids (Protochips) were plasma cleaned for 30 sec with an air mixture in a Gatan Solarus plasma cleaner. Purified complex at ~3mg/ml in HEPES pH7.4, 200mM KCl, 0.4mM DDM was plunge-frozen using a FEI Vitrobot, operated at 100% humidity, 22°C, blot force of 3, and blot time of 3 sec. Grids were imaged on an FEI Talos 200kV microscope equipped with a Falcon II detector. Data were collected semi-automatically using Serial EM [39 (link)], with a pixel size of 1.936 Å, and a total dose of 68 e⁻/Å² fractionated across 40 frames.
Whole-frame drift correction was performed using MotionCor2 [40 (link)], and data were further processed using Eman2 [41 (link)]. Approximately 6000 particles were manually picked for KcsA-Fab4 elbow variant, CTF corrected and classified in 2D. The best 1500 “top view” particles were selected and averaged.

Bailey L.J., Sheehy K.M., Dominik P.K., Liang V., Rui H., Clark M., Jaskolowski M., Kim Y., Deneka D., Tang W.J, & Kossiakoff A.A. (2017). Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. Journal of molecular biology, 430(3), 337-347.

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Cryo-EM Sample Preparation Protocol

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The apoferritin and aldolase samples imaged on the Talos F200C microscope were prepared on UltrAuFoil holey carbon grids (300 mesh, 1.2/1.3 μm spacing) purchased from Quantifoil. Grids were plasma cleaned for six seconds at 15 Watts (75% nitrogen/25% oxygen atmosphere) using a Solarus plasma cleaner (Gatan, Inc.) immediately prior to sample preparation, which was performed using a custom-built manual plunger located in a cold room (≥95% relative humidity, 4 °C). 3 μL of purified aldolase (1.6 mg/mL) or apoferritin (5 mg/mL) was applied to grids and manually blotted for four to five seconds using Whatman No. 1 filter paper. Blot time counting commenced once the blotted sample on the filter paper stopped spreading, monitored visually using a lamp positioned behind the sample. At the end of 4-5 s, the blotting paper was pulled back and immediately plunged into a well of liquid ethane cooled by liquid nitrogen.

Chan L.M., Courteau B.J., Maker A., Wu M., Basanta B., Mehmood H., Bulkley D., Joyce D., Lee B.C., Mick S., Gulati S., Lander G.C, & Verba K.A. (2024). High-resolution single-particle imaging at 100-200 keV with the Gatan Alpine direct electron detector. bioRxiv.

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Cryo-EM Grid Preparation for Amphipol, Nanodisc, and LMNG-stabilized Proteins

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UltraAuFoil R1.2/1.3 300-mesh grids (Quantifoil) were cleaned with a 75% argon/25% oxygen gas at 15 Watts for 7s in a Solarus plasma cleaner (Gatan, Inc.). Cryo-EM grids were prepared in a cold room with a relative humidity of ~88%. A 3 μl aliquot of a protein sample (12 mg/ml amphipol-stabilized ATG9A, 9 mg/ml nanodisc-embedded ATG9A, or 3 mg/ml LMNG-solubilized ATG9A) was dispensed on a cleaned grid and incubated for ~10s. Then, the grid was blotted for ~3–4 s with a Whatman No. 1 filter paper manually and immediately dropped into liquid nitrogen-cooled liquid ethane using a custom-made plunger. Grids were transferred to a storage box and stored in liquid nitrogen until use.
Cryo-EM grids were screening on 200 keV transmission electron microscopes with side-entry cryo-holders. Visual inspection of micrographs suggested that the amphipols and nanodisc samples exhibited moderately preferred orientations (near top views), but the LMNG sample showed mostly top views. To alleviate the heavily preferred orientation and improve the overall quality of the LMNG grids, CHAPS was added to the LMNG sample immediately prior to grid preparation.

Maeda S., Yamamoto H., Kinch L.N., Garza C.M., Takahashi S., Otomo C., Grishin N.V., Forli S., Mizushima N, & Otomo T. (2020). Structure, lipid scrambling activity and role in autophagosome formation of ATG9A. Nature structural & molecular biology, 27(12), 1194-1201.

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Cryo-EM Sample Preparation for TFIID-IIA-SCP

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Cryo-EM samples were prepared on continuous carbon coated C-flat holey carbon grids (Protochips). Grids were plasma cleaned for 10 s in air using a Solarus Plasma Cleaner (Gatan) operating at 10 Watts. Immediately following crosslinking, 4 μl of purified TFIID-IIA-SCP complex or TAF-less PIC was added to the plasma-cleaned grid and loaded into a Vitrobot (FEI). The sample was incubated on the grid for 10 minutes at 4 °C and 100% relative humidity to enhance its absorption onto the carbon substrate, then was blotted and immediately plunge-frozen in liquid ethane. Frozen grids were transferred to a 626 Cryo-Transfer Holder (Gatan) and loaded into a Titan electron microscope (FEI) operating at 300 keV. Images were recorded with a K2 direct electron detector (Gatan) operating in counting mode at a calibrated magnification of 37,879 (1.32 Å pixel⁻¹) and a defocus range of −2 μm to −4 μm, using the Leginon data collection software for semi-automated acquisition targeting. 20-frame exposures were taken at 0.5 s per frame (10 s total exposure time), using a dose rate of 8 e⁻ pixel⁻¹ s⁻¹ (4.6 e⁻ Å⁻² s⁻¹ or 2.3 e⁻ Å⁻² per frame), corresponding to a total dose of 46 e⁻ Å⁻² per micrograph.

Louder R.K., He Y., López-Blanco J.R., Fang J., Chacón P, & Nogales E. (2016). Structure of promoter-bound TFIID and insight into human PIC assembly. Nature, 531(7596), 604-609.

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Negative Staining of PI3KC3 Complexes

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Negatively stained samples of PI3KC3-C1 and -C2 were prepared on continuous carbon grids that had been plasma cleaned in a 10% O₂ atmosphere for 10 s using a Solarus plasma cleaner (Gatan Inc., Pleasanton, CA). 4 μl of PI3KC3 complexes at a concentration of 25 nM in 20 mM Tris, pH 8.0, 200 mM NaCl, 2 mM MgCl₂, 1 mM TCEP, and 3% trehalose were placed on the grids and incubated for 30 s. The grids were floated on four successive 50 μl drops of 1% uranyl formate solution incubating for 10 s on each drop. The stained grids were blotted to near dryness with a filter paper and air-dried.

Baskaran S., Carlson L.A., Stjepanovic G., Young L.N., Kim D.J., Grob P., Stanley R.E., Nogales E, & Hurley J.H. (2014). Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex. eLife, 3, e05115.

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Cryo-EM Sample Preparation for mSerRS-mtRNA Complex

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The human mSerRS-mtRNA^Ser(UGA) complex was diluted to a concentration of 0.75 mg/ml and samples were mixed with 0.05% v/v Lauryl Maltose Neopentyl Glycol (Anatrace) immediately prior to plunge freezing. UltrAuFoil R1.2/1.3 300-mesh grids (Quantifoil) were plasma cleaned in a Solarus plasma cleaner (Gatan, Inc.) with a 75% nitrogen, 25% oxygen atmosphere at 15 W for 7 s. Cryo-EM grids were prepared by application of 4 μL protein sample at 4 °C in 95% humidity. The grids were manually blotted for 4-5 s using Whatman No. 1 filter paper, followed by plunge freezing in liquid ethane.

Kuhle B., Hirschi M., Doerfel L.K., Lander G.C, & Schimmel P. (2023). Structural basis for a degenerate tRNA identity code and the evolution of bimodal specificity in human mitochondrial tRNA recognition. Nature Communications, 14, 4794.

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