60 ti rotor

Manufactured by Beckman Coulter

Sourced in United States, Canada

The An-60 Ti rotor is a high-performance centrifuge rotor designed for use with Beckman Coulter's centrifuge systems. It is made of titanium, providing excellent strength and corrosion resistance. The An-60 Ti rotor is capable of achieving high rotational speeds, making it suitable for a variety of laboratory applications that require efficient separation and processing of samples.

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SW 60 Ti swinging-bucket rotor (15 citations) Four-hole An-60 Ti rotor (11 citations) AN-60 rotor (3 citations) Type 60 Ti rotor (3 citations) AN-60 Ti four-hole rotor (3 citations) 60 Ti fixed angle rotor (2 citations) 4-hole An-60 Ti rotor (2 citations) ProteomeLab™ XL-A/XL-I An-60 Ti rotor (2 citations)

111 protocols using 60 ti rotor

Sedimentation-Velocity Analysis of S-Crystallin

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The experiments were performed on an XL-A analytical ultracentrifuge using an An-60 Ti rotor (Beckman Coulter)34 (link)35 (link)36 (link). The sedimentation-velocity experiments were performed using a double-sector epon charcoal-filled centerpiece at 20 °C with a rotor speed of 42,000 rpm. Protein solutions of S-crystallin and its mutants (0.025–1.0 mg/ml) and a reference buffer (50 mM phosphate, pH 6.5) were loaded into the centerpiece. The absorbance at 230 or 280 nm was monitored in continuous mode with a time interval of 300 s and a step size of 0.003 cm. Multiple scans at different time intervals were then fitted to a continuous c(M) distribution model using SEDFIT37 (link)38 (link).

Tan W.H., Cheng S.C., Liu Y.T., Wu C.G., Lin M.H., Chen C.C., Lin C.H, & Chou C.Y. (2016). Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive Protein. Scientific Reports, 6, 31176.

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Sedimentation Velocity Analysis of DdrC

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Sedimentation velocity experiments were performed at 42 000 rpm and 4°C, on a Beckman XLI analytical ultracentrifuge using a AN-60 Ti rotor (Beckman Coulter, Brea, USA) and double-sector cells with optical path lengths of 12 and 1.5 mm equipped with sapphire windows (Nanolytics, Potsdam, DE). Buffer C was used as a reference. Measurements were made on 1, 4 and 8 mg.ml^–1 DdrC using absorbance at 280 nm and interference optics. Data were processed with the REDATE software (https://www.utsouthwestern.edu/labs/mbr/software/) and the parameters were determined with SEDNTERP and SEDFIT (53 (link)). Analysis of sedimentation coefficients and molecular weights were performed using SEDFIT (53 (link)) and GUSSI (54 (link)).

Banneville A.S., Bouthier de la Tour C., De Bonis S., Hognon C., Colletier J.P., Teulon J.M., Le Roy A., Pellequer J.L., Monari A., Dehez F., Confalonieri F., Servant P, & Timmins J. (2022). Structural and functional characterization of DdrC, a novel DNA damage-induced nucleoid associated protein involved in DNA compaction. Nucleic Acids Research, 50(13), 7680-7696.

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Sedimentation Velocity Analysis of RNA Compaction

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Sedimentation velocity analytical ultracentrifugation (SV-AUC) experiments were performed using a Beckman XL-1 centrifuge with An-60 Ti rotor (Beckman Coulter). Prior to centrifugation, RNA was supplemented with 25 mM K-HEPES pH 7.0, 150 mM KCl, 0.1 mM Na-EDTA, and appropriate MgCl₂ concentrations as indicated in the results section, and incubated for 45 minutes at 37°C. RNA concentrations were adjusted to obtain an initial absorption value of 0.4 at 260 nm on the instrument. All experiments were performed at 20 °C at 25,000 rpm, and independently repeated once. Data were analyzed using the continuous c(s) distribution model as implemented in Sedfit^{43 (link),44 (link)}. Hydrodynamic radii (R_h) were calculated assuming a partial specific volume of 0.53 cm³/g and a hydration of 0.59 g/g in Sedfit^{36 (link)}. Hill plots were drawn for each set of data in Prism (GraphPad).
It’s important to note that the homogeneity of RNA samples is not evaluated by the shape of the sedimentation curve itself, but by mathematically fitting the calculated molecule radii to the Hill equation in order to obtain a value of K_{1/2 Mg}. At the Mg²⁺ concentration indicated by a particular K_{1/2 Mg} value, 50% of the RNA molecules are compacted. Therefore, we chose 15 mM Mg²⁺ (more than 3 times of the K_{1/2 Mg} value) to obtain a completely compact and monodisperse form of RepA.

Liu F., Somarowthu S, & Pyle A.M. (2017). Visualizing the secondary and tertiary architectural domains of lncRNA RepA. Nature chemical biology, 13(3), 282-289.

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Analytical Ultracentrifugation of Rad50 Complexes

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Molecular mass of the Rad50HCC182 was analyzed with an Optima XL-A analytical ultracentrifuge (Beckman). Sedimentation equilibrium data were evaluated using a nonlinear least-squares curve-fitting algorithm (XL-A data analysis software). Samples (40 µM) were analyzed in a buffer B (25 mM Tris-HCl pH 7.4, 150 mM NaCl, 5 mM β-mercaptoethanol) for Rad50HCC182, SMC hinge, Pfhook, ΔCC, and ΔCC-48 or buffer C (buffer B with 0.5 mM EDTA) for Zn²⁺-free Rad50HCC182. To prepare Zn²⁺ free Rad50HCC182, sample was dialyzed in a buffer C for at least 24 hrs. Data were collected at 11,000, 14,000, 25,000, 35,000, and 37,000 rpm to optimize the detection of dimeric and monomeric Rad50HCC182 mutants and 15°C using an An60Ti rotor (Beckman) and by measuring the absorbance at 280 nm. The partial specific volume of Rad50HCC182 was estimated to be 0.731 cm³/g from the protein sequence using the SEDNTERP program, and a rho value of 1.005 was used for the molecular mass calculation. The partial specific volume of SMC hinge, Pfhook, ΔCC, and ΔCC-48 were estimated to be 0.738, 0.734, 0.722, and 0.721 cm³/g, respectively.

Park Y.B., Hohl M., Padjasek M., Jeong E., Jin K.S., Krężel A., Petrini J.H, & Cho Y. (2017). Eukaryotic Rad50 Functions as A Rod-shaped Dimer. Nature structural & molecular biology, 24(3), 248-257.

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Analytical Ultracentrifugation of Protein Constructs

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A Beckman Optima XL-I analytical ultracentrifuge, absorption optics, an An-60 Ti rotor and standard double-sector centerpiece cells were used. Equilibrium measurements for the various constructs were made at 20 °C using the centrifuge speeds shown in Table 1. Concentration profiles were recorded every 4 h for 16 h, and then baselines were established by overspeeding at 45 000 rpm for 3 h. Data (the average of 8–10 scans collected using a radial step size of 0.001 cm) were analyzed using the standard Optima XL-I data analysis software. Sedimentation velocity experiments were performed at 40 000 rpm with scans recorded every 6 min for 3 h. Protein partial specific volumes (ν-bar), calculated from the amino acid compositions, and solvent densities were estimated using the program SEDNTERP (http://www.rasmb.bbri.org/). The ν-bar values are shown in Table 1.

Watts N.R., Zhuang X., Kaufman J.D., Palmer I.W., Dearborn A.D., Coscia S., Blech-Hermoni Y., Alfano C., Pastore A., Mankodi A, & Wingfield P.T. (2017). Expression and Purification of ZASP Subdomains and Clinically Important Isoforms: High-Affinity Binding to G-Actin. Biochemistry, 56(14), 2061-2070.

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Sedimentation Velocity Analysis of Proteins

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A Beckman Optima XL-I analytical ultracentrifuge, absorption optics, an An-60 Ti rotor, and standard double-sector centerpiece cells were used. Sedimentation velocity measurements of samples at 1 mg/mL, at 20 °C, were made at 40,000 rpm with data collection every 8 min to 3 h. Data analysis was done using DCDT+ 2.4.3. [41 (link)]. Correction of the sedimentation coefficient was made using protein partial specific volumes (ν-bar), calculated from the amino acid compositions, and solvent densities were estimated using the program SEDNTERP (http://www.rasmb.bbri.org/).

Dolinska M.B., Young KL I.I., Kassouf C., Dimitriadis E.K., Wingfield P.T, & Sergeev Y.V. (2020). Protein Stability and Functional Characterization of Intra-Melanosomal Domain of Human Recombinant Tyrosinase-Related Protein 1. International Journal of Molecular Sciences, 21(1), 331.

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Sedimentation Velocity and Equilibrium Studies of OPA1-MGD

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For each run, 25 µM OPA1-MGD was used in buffer containing 25 mM Hepes (pH 7.4), 250 mM KCl, and 4 mM MgCl₂. Sedimentation velocity experiments were performed at 20°C in a ProteomeLab XL-1 Protein Characterization System (Beckman Coulter), except for 217-MGD at 10°C. All interference data were collected at 42,000 rpm using an An-60 Ti rotor (Beckman Coulter). The AUC data were processed according to a concentration (sedimentation coefficient) distribution model. For sedimentation equilibrium experiments, OPA1-MGD was prepared at three different concentrations (10, 15, and 20 µM). Interference data were collected at three different speeds (12,000, 19,000, and 24,000 rpm) in an An-60 Ti rotor at 10°C and analyzed by SEDPHAT using the monomer–dimer association model.

Yu C., Zhao J., Yan L., Qi Y., Guo X., Lou Z., Hu J, & Rao Z. (2020). Structural insights into G domain dimerization and pathogenic mutation of OPA1. The Journal of Cell Biology, 219(7), e201907098.

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Analytical Ultracentrifugation of Superparamagnetic Iron Oxide Nanoparticles

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The total loading sample average sedimentation coefficients of both brand and generic SFG products were measured by analytical ultracentrifugation (AUC). In order to determine lot to lot variation, three different lots of both brand SFG and generic SFG were used during this experiment. SFG samples were diluted to a 2.2 mM Fe total iron concentration in 0.9% NaCl solution prior to AUC measurement. AUC was performed using a Beckman Optima XL-A, An-60 Ti rotor, scanning absorbance optics, with 12 mm path length double sector graphite centerpieces and quartz lenses. All measurements were made at 470 nm at a speed of 42,000 rpm, 20 °C. Data collected over 100 scans were used as a representation of the whole run (radial step size of 0.003 cm). The total loading sample sedimentation coefficients of both brand and generic SFG samples for each concentration were calculated by integrating 100% of the loading concentration signal using an ls-g*(s) SEDFIT model where both RI noise and time-independent noise were accounted for. To ensure that the total loading sample sedimentation coefficients were not concentration-dependent, SFG samples were also diluted to four other total iron concentrations (0.9, 1.5, 1.8, and 2.6 mM Fe) in 0.9% NaCl solution and analyzed via AUC.

Brandis J.E., Kihn K.C., Taraban M.B., Schnorr J., Confer A.M., Batelu S., Sun D., Rodriguez J.D., Jiang W., Goldberg D.P., Langguth P., Stemmler T.L., Yu Y.B., Kane M.A., Polli J.E, & Michel S.L. (2021). Evaluation of the Physicochemical Properties of the Iron Nanoparticle Drug Products: Brand and Generic Sodium Ferric Gluconate. Molecular pharmaceutics, 18(4), 1544-1557.

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Sedimentation Analysis of Viral-Like Particles

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Sedimentation analysis was carried out on a Beckman XL-A analytical ultracentrifuge at 20 °C. 10 mM phosphate buffer pH 6.5 with 0.5 M NaCl was used as the reference solution. WT and chimeric VLPs were diluted to 0.5 mg/mL with reference solution, and centrifuged at 3951 × g using an An-60 Ti rotor (Beckman Coulter; Fullerton, CA). The sedimentation coefficient was determined using Sedfit software kindly provided by Dr. P. Schuck at the National Institutes of Health (Bethesda, MD).

Qian C., Yang Y., Xu Q., Wang Z., Chen J., Chi X., Yu M., Gao F., Xu Y., Lu Y., Sun H., Shen J., Wang D., Zhou L., Li T., Wang Y., Zheng Q., Yu H., Zhang J., Gu Y., Xia N, & Li S. (2022). Characterization of an Escherichia coli-derived triple-type chimeric vaccine against human papillomavirus types 39, 68 and 70. NPJ Vaccines, 7, 134.

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Protein and RNA Sedimentation Analysis

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A Beckman Optima XL-1 analytical ultracentrifuge, absorption optics, an An-60 Ti rotor, and standard, double-sector centerpiece cells were used. Sedimentation velocity runs were made at 15°C at 40,000 rpm. Absorbance scans at 260 and 280 were performed every 8 minutes for 3 hours. Protein and RNA samples were in 50 mM sodium phosphate, pH 7.5, 150 mM sodium chloride.

Dearborn A.D., Eren E., Watts N.R., Palmer I.W., Kaufman J.D., Steven A.C, & Wingfield P.T. (2018). Structure of an RNA Aptamer that Can Inhibit HIV-1 by Blocking Rev-Cognate RNA (RRE) Binding and Rev-Rev Association. Structure (London, England : 1993), 26(9), 1187-1195.e4.

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