Transmission Electron Microscope

Titan Krios TEM for Life Sciences

Tailored for use in protein and cellular imaging

The FEI Titan Krios transmission electron microscope's (TEM) revolutionary cryo-based technology and stability permits a full range of semi-automated applications, including 2D electron crystallography, single particle analysis, cryo electron microscopy, and dual-axis cellular tomography of frozen hydrated cell organelles and cells. Cryo techniques preserve sample integrity by maintaining the sample in its natural condition and state. The Titan Krios TEM's versatility ensures that you will be able to perform today's experiments, as well as addressing new research problems in the future. Choose from a broad variety of detector and software options to configure the Titan Krios TEM for any of these applications.




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The most powerful and flexible high-resolution electron microscope for 2D and 3D characterization of biological samples

The Titan Krios TEM optimal thermal and mechanical stability ensures perfect optical performance. The Titan Krios TEM enables days of unattended operation, which, when combined with the automated sample loader, results in unprecedented sample throughput.

The Titan Krios TEM Benefits for structural biology

  • Reduced time to data and reduced cost per structure enabled by automated sample loader and long unattended operation
  • Robotic loading of up to 12 frozen, hydrated samples for increased throughput
  • Reduced installation and operating requirements: environmental instrument enclosure provides optimal thermal and acoustic shielding
  • Optimized connectivity to latest hardware and software developments
  • Minimal thermal drift due to ConstantPower™ lenses


 

 

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Titan Krios datasheet

The Titan Krios transmission electron microscope (TEM) is tailored for use in protein and cellular imaging. Its revolutionary cryo-based technology and stability permits a full range of semi-automated applications, including: 2D electron crystallography, single particle analysis, cryo electron microscopy, and dual-axis cellular tomography of frozen hydrated cell organelles and cells.

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Publication list for Titan Krios for Life Sciences

Title: Single-protein detection in crowded molecular environments in cryo-EM images
Authors: Rickgauer, J.P., Grigorieff, N. and Denk, W. 
References: eLife Vol. 6 (2017)
DOI10.7554/eLife.25648
Date: May 2017
Abstract
Title: Single-protein detection in crowded molecular environments in cryo-EM images
Authors: Rickgauer, J.P., Grigorieff, N. and Denk, W. 
References: eLife Vol. 6 (2017)
DOI10.7554/eLife.25648
Date: May 2017
Abstract: We present an approach to study macromolecular assemblies by detecting component proteins' characteristic high-resolution projection patterns, calculated from their known 3D structures, in single electron cryo-micrographs. Our method detects single apoferritin molecules in vitreous ice with high specificity and determines their orientation and location precisely. Simulations show that high spatial-frequency information and-in the presence of protein background-a whitening filter are essential for optimal detection, in particular for images taken far from focus. Experimentally, we could detect small viral RNA polymerase molecules, distributed randomly among binding locations, inside rotavirus particles. Based on the currently attainable image quality, we estimate a threshold for detection that is 150 kDa in ice and 300 kDa in 100 nm thick samples of dense biological material.
Title: Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
Authors: Ichikawa, M., Liu, D., Kastritis, P.L., Basu, K., Hsu, T.C., Yang, S. and Bui, K.H. 
References: Nature communications Vol. 8, pp. 15035 (2017)
DOI10.1038/ncomms15035
Date: May 2017
Abstract
Title: Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins
Authors: Ichikawa, M., Liu, D., Kastritis, P.L., Basu, K., Hsu, T.C., Yang, S. and Bui, K.H. 
References: Nature communications Vol. 8, pp. 15035 (2017)
DOI10.1038/ncomms15035
Date: May 2017
Abstract: Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign α- and β-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule.
Title: An Atomic Structure of the Human Spliceosome
Authors: Zhang, X., Yan, C., Hang, J., Finci, L.I., Lei, J. and Shi, Y. 
References: Cell (2017)
Date: May 2017
Abstract
Title: An Atomic Structure of the Human Spliceosome
Authors: Zhang, X., Yan, C., Hang, J., Finci, L.I., Lei, J. and Shi, Y. 
References: Cell (2017)
DOI10.1016/j.cell.2017.04.033
Date: May 2017
Abstract: Mechanistic understanding of pre-mRNA splicing requires detailed structural information on various states of the spliceosome. Here we report the cryo electron microscopy (cryo-EM) structure of the human spliceosome just before exon ligation (the C* complex) at an average resolution of 3.76 Å. The splicing factor Prp17 stabilizes the active site conformation. The step II factor Slu7 adopts an extended conformation, binds Prp8 and Cwc22, and is poised for selection of the 3'-splice site. Remarkably, the intron lariat traverses through a positively charged central channel of RBM22; this unusual organization suggests mechanisms of intron recruitment, confinement, and release. The protein PRKRIP1 forms a 100-Å α helix linking the distant U2 snRNP to the catalytic center. A 35-residue fragment of the ATPase/helicase Prp22 latches onto Prp8, and the quaternary exon junction complex (EJC) recognizes upstream 5'-exon sequences and associates with Cwc22 and the GTPase Snu114. These structural features reveal important mechanistic insights into exon ligation.
Title: Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial Conjugation
Authors: Ilangovan, A., Kay, C.W.M., Roier, S., El Mkami, H., Salvadori, E., Zechner, E.L., Zanetti, G. and Waksman, G. 
References: Cell (2017)
Date: April 2017
Abstract
Title: Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial Conjugation
Authors: Ilangovan, A., Kay, C.W.M., Roier, S., El Mkami, H., Salvadori, E., Zechner, E.L., Zanetti, G. and Waksman, G. 
References: Cell (2017)
DOI10.1016/j.cell.2017.04.010
Date: April 2017
Abstract: Relaxases play essential roles in conjugation, the main process by which bacteria exchange genetic material, notably antibiotic resistance genes. They are bifunctional enzymes containing a trans-esterase activity, which is responsible for nicking the DNA strand to be transferred and for covalent attachment to the resulting 5’-phosphate end, and a helicase activity, which is responsible for unwinding the DNA while it is being transported to a recipient cell. Here we show that these two activities are carried out by two conformers that can both load simultaneously on the origin of transfer DNA. We solve the structure of one of these conformers by cryo electron microscopy to near-atomic resolution, elucidating the molecular basis of helicase function by relaxases and revealing insights into the mechanistic events taking place in the cell prior to substrate transport during conjugation.