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.




Need more information?

Contact a Sales or Service Representative

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


 

 

Featured Accessory

Themis Upgrades & Accessories

Designed to update and enhance the capabilities of your Themis

FEI has continuously increased the capabilities of the Themis product family. We can offer to each Themis user upgrades to the latest available technology.

See accessory

Featured Document

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.

Download document

Publication list for Titan Krios for Life Sciences

Title: The structure of the yeast mitochondrial ribosome
Authors: Desai, N., Brown, A., Amunts, A. and Ramakrishnan, V. 
References: Science Vol. 355(6324), pp. 528-531 (2017) 
DOI10.1126/science.aal2415
Date: February 2017
Abstract
Title: The structure of the yeast mitochondrial ribosome
Authors: Desai, N., Brown, A., Amunts, A. and Ramakrishnan, V. 
References: Science Vol. 355(6324), pp. 528-531 (2017) 
DOI10.1126/science.aal2415
Date: February 2017
Abstract: Mitochondria have specialized ribosomes (mitoribosomes) dedicated to the expression of the genetic information encoded by their genomes. Here, using electron cryomicroscopy, we have determined the structure of the 75-component yeast mitoribosome to an overall resolution of 3.3 angstroms. The mitoribosomal small subunit has been built de novo and includes 15S ribosomal RNA (rRNA) and 34 proteins, including 14 without homologs in the evolutionarily related bacterial ribosome. Yeast-specific rRNA and protein elements, including the acquisition of a putatively active enzyme, give the mitoribosome a distinct architecture compared to the mammalian mitoribosome. At an expanded messenger RNA channel exit, there is a binding platform for translational activators that regulate translation in yeast but not mammalian mitochondria. The structure provides insights into the evolution and species-specific specialization of mitochondrial translation. 
Title: Structural snapshot of cytoplasmic pre-60S ribosomal particles bound by Nmd3, Lsg1, Tif6 and Reh1.
Authors: Ma, C., Wu, S., Li, N., Chen, Y., Yan, K., Li, Z., Zheng, L., Lei, J., Woolford, J.L. and Gao, N. 
References: Nature structural & molecular biology (2017)  
DOI10.1038/nsmb.3364
Date: January 2017
Abstract
Title: Structural snapshot of cytoplasmic pre-60S ribosomal particles bound by Nmd3, Lsg1, Tif6 and Reh1.
Authors: Ma, C., Wu, S., Li, N., Chen, Y., Yan, K., Li, Z., Zheng, L., Lei, J., Woolford, J.L. and Gao, N. 
References: Nature structural & molecular biology (2017)  
DOI10.1038/nsmb.3364
Date: January 2017
Abstract: A key step in ribosome biogenesis is the nuclear export of pre-ribosomal particles. Nmd3, a highly conserved protein in eukaryotes, is a specific adaptor required for the export of pre-60S particles. Here we used cryo-electron microscopy (cryo-EM) to characterize Saccharomyces cerevisiae pre-60S particles purified with epitope-tagged Nmd3. Our structural analysis indicates that these particles belong to a specific late stage of cytoplasmic pre-60S maturation in which ribosomal proteins uL16, uL10, uL11, eL40 and eL41 are deficient, but ribosome assembly factors Nmd3, Lsg1, Tif6 and Reh1 are present. Nmd3 and Lsg1 are located near the peptidyl-transferase center (PTC). In particular, Nmd3 recognizes the PTC in its near-mature conformation. In contrast, Reh1 is anchored to the exit of the polypeptide tunnel, with its C terminus inserted into the tunnel. These findings pinpoint a structural checkpoint role for Nmd3 in PTC assembly, and provide information about functional and mechanistic roles of these assembly factors in the maturation of the 60S ribosomal subunit. 
Title: Cryo-EM structure of a human spliceosome activated for step 2 of splicing.
Authors: Bertram, K., Agafonov, D.E., Liu, W.-T., Dybkov, O., Will, C.L., Hartmuth, K., Urlaub, H., Kastner, B., Stark, H. and Lührmann, R. 
References: Nature (2017)
Date: January 2017
Abstract
Title: Cryo-EM structure of a human spliceosome activated for step 2 of splicing.
Authors: Bertram, K., Agafonov, D.E., Liu, W.-T., Dybkov, O., Will, C.L., Hartmuth, K., Urlaub, H., Kastner, B., Stark, H. and Lührmann, R. 
References: Nature (2017)
DOI10.1038/nature21079
Date: January 2017
Abstract: Spliceosome rearrangements facilitated by RNA helicase Prp16 before catalytic step 2 of splicing are poorly understood. Here we report a 3D cryo-electron microscopy structure of the human spliceosomal C complex stalled directly after Prp16 action (C*). The architecture of the catalytic U2-U6 RNP core of the human C* spliceosome is highly similar to that of the yeast pre-Prp16 C complex. However, in C* the branched intron region is separated (by  20 Å) from the catalytic centre, and its position close to the U6 snRNA ACAGA box is stabilised by interactions with the Prp8 RNase H-like and Prp17 WD40 domains. RNA helicase Prp22 is located about 100 Å from the catalytic centre, suggesting that it destabilises the spliced mRNA after step 2 from a distance. Comparison of the structure of the yeast C and human C* complexes reveals numerous RNP rearrangements that are likely to be facilitated by Prp16, including a large-scale movement of the U2 snRNP.
Title: Self-correcting mismatches during high-fidelity DNA replication.
Authors: Fernandez-Leiro, R., Conrad, J., Yang, J.-C., Freund, S.M.V., Scheres, S.H.W. and Lamers, M.H. 
References: Nature structural & molecular biology (2017)  
Date: January 2017
Abstract
Title: Self-correcting mismatches during high-fidelity DNA replication.
Authors: Fernandez-Leiro, R., Conrad, J., Yang, J.-C., Freund, S.M.V., Scheres, S.H.W. and Lamers, M.H. 
References: Nature structural & molecular biology (2017)  
DOI10.1038/nsmb.3348
Date: January 2017
Abstract: Faithful DNA replication is essential to all forms of life and depends on the action of 3'-5' exonucleases that remove misincorporated nucleotides from the newly synthesized strand. However, how the DNA is transferred from the polymerase to the exonuclease active site is not known. Here we present the cryo-EM structure of the editing mode of the catalytic core of the Escherichia coli replisome, revealing a dramatic distortion of the DNA whereby the polymerase thumb domain acts as a wedge that separates the two DNA strands. Importantly, NMR analysis of the DNA substrate shows that the presence of a mismatch increases the fraying of the DNA, thus enabling it to reach the exonuclease active site. Therefore the mismatch corrects itself, whereas the exonuclease subunit plays a passive role. Hence, our work provides unique insights into high-fidelity replication and establishes a new paradigm for the correction of misincorporated nucleotides.