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CryoEM core facility

Biocenter Finland / HiLIFE / Instruct-FI National facility for Cryo Electron-microscopy

Open to both academic and commercial users
Situated in the Institute of Biotechnology in the University of Helsinki
Managed by Sarah Butcher

Service Poster

Part of: Biocenter Finland, Hilife and Instruct-FI.


Microscope Engineer for external projects Pasi Laurinmäki 02941 59502

Research Assistant for external projects Benita Löflund 02941 59502

Instructions how to start a new project (22.5.2017):

1.Contact Pasi or Benita (grp-cryoemservice at helsinki dot fi), or the Instruct-Fi coordinators (Hanna Oksanen, Katri Eskelin – first name dot last name at helsinki dot fi).

2. Have a kickoff meeting.

3.Fill in an application form for a new project. This will help scientific review of your project. If accepted, you will receive a unique ID that you will use for reservations, samples etc. Project sheet Cryo-EM-Unit

4.Once sample delivery has been agreed, fill in the eform for sample delivery using your unique identifier. This will be used for billing, so keep the number to yourself. Link to Eform

5. Samples are brought to Biocenter 1, EM unit floor and delivered to Pasi Laurinmäki or Benita Löflund at an agreed date and time.

6. Samples are made and images are collected and delivered to the customer.

7. Billing is 3 times a year.

Diamond Light Source/iNEXT Cryo specimen preparation course 2017The course was a great success, We aim to run a similar course in Helsinki in summer  2017 for the ILS graduate programme

Course dates: 28-30th August 2017 Cryo-specimen preparation course (12 PhD students from ILS; upto 3 additional external participants with fee of 400€ to cover materials and instructors; does not include accommodation or meals)

Course dates: 30th August- 1st September 2017 Cryo-EM image processing course (12 PhD students from ILS; upto 3 additional external participants with fee of 400€ to cover materials and instructors; does not include accommodation or meals)

NEW: FEI Talos Artica transmission electron microscope with phase plate and direct electron detector (Falcon 3)  installed April 2017.


1) project planning and assessment

2) courses in structural biology, cryo electron microscopy and image reconstruction (Introductory lecture course each September), short advanced courses

3) sample optimisation and preparation with a
Leica vitrification robot EM GP
capable of temperature and humidity control.

Manual vitrification guillotine in biosafety laboratory level 2

Linkam-Zeiss correlative fluorescence light microscopy  for vitrified specimens. This can be used to detect fluorescence in vitrified specimens prior to their being put in the EM. The region of interest can then be rapidly located in the EM for instance to use in electron tomography.

4) Cryo-electron microscopy on an
FEI Artica  equipped with a Falcon III direct electron detector camera and FEI phase plate. Data can be transferred to the CSC Ltd for processing of frames, or returned on a USB drive.FEI Talos Arctica

and on an FEI tecnai F20 with Gatan Ultrascan CCD camera
using gatan 626, gatan 914 (high tilt tomography) and oxford CT3500 cryoholders.

5) advice on image reconstruction

6) collaborative projects

7) PRICE LIST 2017


Recent publications:

Alhoranta, A., Lehtinen, J., Urtti, A., Butcher, S.J., Aseyev, V., Tenhu, H. (2011) Cationic amphiphilic star and linear block copolymers: synthesis, self-assembly and in vitro gene transfection. Biomacromolecules 12;3213

Dearborn, A.D., Laurinmäki, P., Chandramouli, P., Rodenburg, C.M., Wang, S., Butcher, S.J., Dokland, T. (2012) Structure and size determination of bacteriophage P2 and P4 procapsids: function of size responsiveness mutations. J. Struct. Biol. 178:215-224

Guryanov, S., Liljeroos, L. Kasaragod, P., Kajander, T., Butcher, S.J. (2015) Crystal structure of the measles virus nucleoprotein core in complex with an N-terminal region of phosphoprotein. J. Virol. 90:2849-57. doi: 10.1128/JVI.02865-15

Hedegaard, S., Nilsson, C., Laurinmäki, P., Butcher, S.J., Urtti, A., Yaghmur, A. (2013) Nanostructured aqueous dispersions of citrem interacting with lipids and PEGylated lipids. RSC Advances 3:24576–24585.

Hetzel,U., Sironen,T., Laurinmäki, P., Liljeroos, L., Patjas, A., Henttonen, H., Vaheri, A., Artelt, A., Kipar, A., Butcher, S.J., Vapalahti O., Hepojoki J. (2013) Isolation, identification and characterization of novel Arenaviruses, the etiological agent of Boid Inclusion Body Disease. J. Virol. 87:20 10918-10935

Hirvonen, S, Karesoja, M., Karjalainen, E., Hietala, S., Laurinmäki, P., Vesanen, E., Butcher, S.J., Tenhu, H. (2013) Colloidal properties and gelation of aqueous dispersions of conductive poly(benzimidazobenzophenanthroline) derivatives. Polymer 54:694-701

Karjalainen, E., Chenna, N., Laurinmäki, P., Butcher, S.J., Tenhu H. (2013) Diblock copolymers consisting of polymerized ionic liquid and poly(N-isopropylacrylamide). Effects of PNIPAM block length and counter ion on self-assembling and thermal properties.  Polym.Chem. 4:1014-1024

Koho, T., Huhti, L., Blazevic, V., Nurminen, K., Butcher, S.J., Laurinmäki, P., Kalkkinen, N., Rönnholm, G., Vesikari, T., Hytönen, V.P., Kulomaa, M.S. (2011) Production and characterization of virus-like particles and the P domain protein of GII.4 norovirus. J. Vir. Methods doi:10.1016/j.jviromet.2011.05.009

Koho, T., Mäntylä,T., Laurinmäki, P., Huhti, L. Butcher, S., Vesikari,T., Kulomaa, M.S., Hytönen, V.P. (2012) Purification of norovirus-like particles (VLPs) by ion exchange chromatography. J. Vir. Methods. 181:6-11.

Kumar, V., Butcher, S.J., Öörni, K., Engelhardt, P., Heikkonen, J., Kaski, K., Ala-Korpela, M., Kovanen, P.T.(2011) Three-dimensional cryoEM reconstruction of native LDL particles to 16å resolution at physiological body temperature PLoS ONE 6(5): e18841. doi:10.1371/journal.pone.0018841.

Leon-Velarde CG, Happonen L, Pajunen M, Leskinen K, Kropinski AM, Mattinen L, Rajtor M, Zur J, Smith D, Chen S, Nawaz A, Johnson RP, Odumeru JA, Griffiths MW, Skurnik M. Yersinia enterocolitica-specific infection by bacteriophages TG1 and ϕR1-RT is dependent on temperature-regulated expression of the phage host receptor OmpF. Appl Environ Microbiol. 2016 Aug 15;82(17):5340-53. doi: 10.1128/AEM.01594-16

Magarkar A, Mele N, Abdel-Rahman N, Butcher S, Torkkeli M, Serimaa R, Paananen A, Linder M, Bunker A. (2014) Hydrophobin film structure for HFBI and HFBII and mechanism for accelerated film formation. PLOS Computational Biology 10.1371/journal.pcbi.1003745

Nilsson, C., Barrios-Lopez, B., Kallinen, A., Laurinmӓki, P., Butcher, S.J., Raki, M., Bergstrӧm, K., Weng Larsen, S., Østergaard, J., Larsen, C., Urtti, A., Airaksinen, A., Yaghmur, A. (2013) SPECT/CT imaging of radiolabeled cubosomes and hexosomes for potential theranostic applications. Biomaterials 34:8491-8503

Pietilä, MK, Atanasova, NS, Manole, V, Liljeroos, L., Butcher, SJ, Oksanen, HM, Bamford, DH. (2012) Virion architecture unifies globally distributed pleolipoviruses infecting halophilic archaea. J. Virol, 86:5067-5079

Pietilä, M.K., Laurinmäki, P., Russell, D.A., Ko, C., Jacobs-Sera, D., Butcher, S.J., Bamford, D.H., Hendrix, R.W. (2013) Insights into head-tailed viruses infecting extremely halophilic archaea. J. Virol. 87:3248-3260

Pietilä, M.K., Laurinmäki, P., Russell, D.A., Ko, C., Jacobs-Sera, D., Hendrix, R.W., Bamford, D.H., Butcher, S.J.. (2013) Structure of the archaeal head-tailed virus HSTV-1 completes the HK97-fold story. Proc. Natl. Acad. Sci. (USA) 110:10604-10609

Russo G, Witos J, Rantamäki AH, Wiedmer SK. (2017) Cholesterol affects the interaction between an ionic liquid and phospholipid vesicles. A study by differential scanning calorimetry and nanoplasmonic sensing. Biochim Biophys Acta. 2017 Dec;1859(12):2361-2372. doi: 10.1016/j.bbamem.2017.09.011. Epub 2017 Sep 11.

Sarin, L.P, Hirvonen, J., Laurinmäki, P., Butcher, S.J., Bamford, D.H., Poranen, M.M. (2012) Bacteriophage ϕ6 nucleocapsid surface protein 8 interacts with virus-specific membrane vesicles containing the major envelope protein 9. J. Virol. 86:5376-5379

M. Sedlák: Homopolymer Self-assembly into Stable Nanoparticles: Concerted Action of Hydrophobic Association and Hydrogen Bonding in Thermoresponsive Poly(alkylacrylic acid)s, J. Phys. Chem. B, 116 (8), 2356–2364, 2012.

Shakeel S., Westerhuis B.M., Domanska, A., Konig, R.I., Matadeen, R., Koster, A.J., Bakker, A.Q., Beaumont, T., Wolthers, K.C., Butcher, S.J. (2016) Multiple capsid-stabilizing interactions revealed in a high-resolution structure of an emerging picornavirus causing neonatal sepsis. Nature Communications 7:11387. doi: 10.1038/ncomms11387.

Shakeel S., Westerhuis B.M., Ora, A., Koen, G., Bakker, A.Q., Claassen, Y., Wagner, K., Beaumont, T., Wolthers, K.C., Butcher, S.J. (2015) Structural basis of human parechovirus neutralization by human monoclonal antibodies. J. Virol. 89:9571-80

Skurnik, M., Hyytiäinen, H., Happonen, L., Kiljuenn, S., Datta, N., Mattinen, L., Williamson, K., Kristo, P., Szeliga, M., Kalin-Mänttätri, L., Ahola-Iivarinen, E., Kalkkinen, N., Butcher S.J. (2012) Characterization of the genome, proteome and structure of yersiniophage φR1-37. J. Virol. 86:12625-12642

Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Sidén-Kiamos I, Sachse C, Kursula I. Structural differences explain diverse functions of Plasmodium actins. PLoS Pathog. 2014 Apr 17;10(4):e1004091.


Recent users:

Christa Nilsson, University of Copenhagen

Mecki Burmester Faculty of Pharmacy, University of Helsinki

Vitaly Khlebnikov, Faculty of Science, University of Helsinki

Jens-Ola Ekström, University of Umeå

Erno Karjalainen, Faculty of Science, University of Helsinki

Sami Hirvonen, Faculty of Science, University of Helsinki

Szymon Wiktorowicz, Faculty of Science, University of Helsinki

Petri Susi, Turku University of Applied Sciences

Juha Vahokoski, University of Oulu

Salla Ruskamo, University of Oulu

Marian Sedlak, Institute of Experimental Physics, Slovak Academy of Sciences

Vesa Hytönen, Institute of Biomedical Technology, University of Tampere

Arto Urtti, Faculty of Pharmacy, University of Helsinki

Alexander Bilibin, St. Petersburg State University

Sarah Butcher, Institute of Biotechnology, University of Helsinki

Eija Jokitalo, Institute of Biotechnology, University of Helsinki

Dennis Bamford, Institute of Biotechnology, University of Helsinki

Paavo Kinnunen, Biomedicum, University of Helsinki

Heikki Tenhu, Faculty of Science, University of Helsinki

Juha Huiskonen, University of Oxford

Varpu Marjomäki, University of Jyväskylä

Marjo Yli-Perttula, University of Helsinki

Ville Paavilainen, University of Helsinki

Carlotta Glackin, City of Hope, CA, USA