K3 bioquantum

Manufactured by Thermo Fisher Scientific

Sourced in United Kingdom

The K3 BioQuantum is a compact and versatile laboratory instrument designed for the quantification of biomolecules. It utilizes a fluorescence-based detection method to provide accurate and precise measurements of various biological samples, including proteins, nucleic acids, and small molecules.

Automatically generated - may contain errors

Lab products found in correlation

6 protocols using k3 bioquantum

Cryo-EM Data Acquisition on Titan Krios

Check if the same lab product or an alternative is used in the 5 most similar protocols

Grids were loaded into a Titan Krios (Thermo Fisher Scientific) operated at 300 kV, equipped with a Gatan K3 BioQuantum direct electron detector. Movies with 50 frames and an accumulated dose of 65 e/Å² were acquired in counting mode using EPU software (Thermo Fisher Scientific) at a magnification of ×105,000, corresponding to a calibrated pixel size of 0.836 Å/pixel with a defocus range of −0.6 to −2.5 µm. A total of 2348 movies were collected over two microscopy sessions at The Netherlands Centre for Electron Nanoscopy (NeCEN). Detailed data acquisition parameters are summarized in Supplementary Fig. 1 and Supplementary Table 1.

Koning R.I., Vader H., van Nugteren M., Grocutt P.A., Yang W., Renault L.L., Koster A.J., Kamp A.C, & Schwertner M. (2022). Automated vitrification of cryo-EM samples with controllable sample thickness using suction and real-time optical inspection. Nature Communications, 13, 2985.

+ Open protocol

+ Expand

SARS-CoV-2 Spike Protein Cryo-EM Sample Preparation

Check if the same lab product or an alternative is used in the 5 most similar protocols

Grid preparation and image collection were performed similarly for all purified native, mutated and disulphide-stabilized SARS2 S proteins. C-Flat 2/2 3C grids (Protochips) were glow-discharged for 45 seconds at 25 mA. 3 μl of freshly purified protein at ~0.2-0.6 mg/ml supplemented with 0.01% octyl-glucoside (OG) was applied to the grids, which were plunge-frozen in liquid ethane using a Vitrobot (Thermo Fisher Scientific). Double loading with side-blotting between loading was performed when the concentration of purified protein was below 0.3 mg/ml (S-R/x2). Grids were stored in liquid nitrogen and loaded into a Titan Krios electron microscope (Thermo Fisher Scientific) operated at 300kV, equipped with a Gatan K3 BioQuantum direct electron detector with the slit retracted. Movies with 48 frames and an accumulated dose of 50 electrons/Å² were acquired in counting mode using SerialEM-3.8.0 ^{37 (link)} at the magnification of 81,000 X, corresponding to a calibrated pixel size of 1.061 Å/pixel. Detailed data acquisition parameters are summarized in Table 1.

Xiong X., Qu K., Ciazynska K.A., Hosmillo M., Carter A.P., Ebrahimi S., Ke Z., Scheres S.H., Bergamaschi L., Grice G.L., Zhang Y., Nathan J.A., Baker S., James L.C., Baxendale H.E., Goodfellow I., Doffinger R, & Briggs J.A. (2020). A thermostable, closed SARS-CoV-2 spike protein trimer.. Nature structural & molecular biology, 27(10), 934-941.

+ Open protocol

+ Expand

Cryo-CLEM Imaging Workflow Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cryo-LM was performed on a Zeiss Axioimager M2 equipped with a Linkam CMS196M. Transparent light and fluorescent image stacks (21 slices every 75 µm) we recorded using an EC PlanNeofluor ×10/0.30 Ph1 objective lens on an AxioCam MR R3 at a pixel size at the sample level of 1 µm × 1 µm. Brightfield images were recorded using a LED light source and fluorescent images were recorded using an HXP 120 V light source using a 38 HE filter set. Maximum intensity projections for both image stacks were made using Zeiss ZEN 3.4 software and overlays were made in Adobe Photoshop 2021. Cryo-CLEM was performed on a Talos Arctica (Thermo Fisher Scientific) operated at 200 keV, equipped with a Gatan K3 BioQuantum direct electron detector. Correlations were performed and images were recorded using MAPS software (Thermo Fisher Scientific).

+ Open protocol

+ Expand

Cryo-EM Structural Determination Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols

Grids were screened using a 200 kV Talos Arctica microscope (Thermo Fisher Scientific) with a K2 Summit direct electron detector at the GW4 Regional Facility for CryoEM in Bristol, UK. A preliminary dataset was recorded and used to determine initial helical parameters. Micrographs used for the final structure were collected on a 300 kV Titan Krios microscope (Thermo Fisher Scientific) with a K3 BioQuantum direct electron detector (Gatan) at the Electron Bio-imaging Centre (eBIC) at Diamond Light Source, UK. Data were collected using EPU software (Thermo Fisher Scientific) with a defocus range from −1.3 to –2.5 μm in 0.3 μm increments. The total dose was 40 electrons/Å² at a magnification of 81 kx, corresponding to a pixel size of 1.10 Å (0.55 Å super-resolution). Further details are shown in Supplementary Table 1.

Conners R., León-Quezada R.I., McLaren M., Bennett N.J., Daum B., Rakonjac J, & Gold V.A. (2023). Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly. Nature Communications, 14, 2724.

+ Open protocol

+ Expand

Cryo-Correlative Light and Electron Microscopy

Check if the same lab product or an alternative is used in the 5 most similar protocols

CryoLM was performed on a Zeiss Axioimager M2 equipped with a Linkam CMS196M. Transparent light and fluorescent image stacks (21 slices every 75 µm) we recorded using a EC PlanNeofluor 10x/0.30 Ph1 objective lens on an AxioCam MR R3 at a pixel size at the sample level of 1 µm x 1 µm. Brightfield images were recorded using a LED light source and fluorescent images were recorded using a HXP 120 V light source using a 38 HE filter set. Maximum intensity projections for both image stacks were made using Zeiss ZEN software and overlays were made in Adobe Photoshop.
Cryo-CLEM was performed on a Talos Arctica (Thermo Fisher Scientific) operated at 200 keV, equipped with a Gatan K3 BioQuantum direct electron detector. Correlations were performed and images were recorded using MAPS software version 3.0 (Thermo Fisher Scientific).

Koning R.I., Vader H., Nugteren M.v., Grocutt P., Yang W., Renault L., Koster A.J., Kamp A.C.F., & Schwertner M. (2021). Automated vitrification of cryo-EM samples with controllable sample thickness using suction and real-time optical inspection.

+ Open protocol

+ Expand

Cryo-EM Data Acquisition for Structural Studies

Check if the same lab product or an alternative is used in the 5 most similar protocols

Grids were loaded into a Titan Krios (Thermo Fisher Scientific) operated at 300kV, equipped with a Gatan K3 BioQuantum direct electron detector. Movies with 50 frames and an accumulated dose of 65 e/Å 2 were acquired in counting mode using EPU software (Thermo Fisher Scientific) at a magnification of 105,000x, corresponding to a calibrated pixel size of 0.836 Å/pixel with a defocus range of -0.6 to -2.5 µm. A total of 2,348 movies were collected over two microscopy sessions at The Netherlands Centre for Electron Nanoscopy (NeCEN). Detailed data acquisition parameters are summarized in Supplementary Figure 1 and Supplementary Table 1.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!