CryoEM

CryoEM is particularly useful for objects that are too large, unstable, or variable to be studied by X-ray crystallography or NMR. It can be used to understand the structure, assembly, and function of various biological macromolecule complexes. The cryoEM data can be used with image processing software to make 3D-models. Training in three-dimensional image reconstruction is given through fortnightly to monthly visits for data processing. Cryo-correlative light and electron microscopy (cryo-CLEM) is a unique national service.

Instruct-ERIC Centre Finland / CryoEM

CryoEM services are part of Instruct-ERIC Centre Finland and can be accessed through Instruct-ERIC (Instruct Centre Finland/CryoEM home page). See funding possibilities for Instruct-ERIC access.

• Basic and advanced cryoEM techniques
• Project planning and assessment
• Sample optimisation and preparation
• Plunge freezing services (BSL2)
• Automated single particle and cryo-tomography digital data collection
• Advice on image reconstruction
• Collaborative projects
• Courses in structural biology, cryo electron microscopy and image reconstruction

CryoEM is applicable for projects in e.g. structural biology, nanotechnology, time-resolved assembly and phase transitions. Depending on the approach used, nanoscale resolution can be achieved.

• Single particle averaging and three dimensional (3D) reconstructions
• Electron tomography and 3D-reconstructions
• Measurements and statistical analyses
• Study of biological macromolecular complexes and other electron-beam sensitive materials in aqueous solutions.
• Particle sizes that range from ~10 to 300 nm in diameter.

Leica vitrification robot EM GP

• Automatic plunge freezer for the bare grid technique that is used for the preparation of vitrified fluid samples or extremely thin samples for cryo-EM.
• Suitable for biological suspensions and industrial emulsions in both, aqueous and inorganic solvents. Typical sample volume per grid 3 µL.
• Can be used to plunge freeze samples not only on EM grids, but also sapphire discs and samples in freeze fracture planchettes.
• Temperature and humidity controlled 4-65 degrees C, ambient to 100% humidity.
• Biosafety laboratory level 2.

Cryosol VitroJet

• Blot-free automatic plunge freezer for clipped bare grid technique that is used for the preparation of vitrified fluid samples for cryo-EM.
• Suitable for biological suspensions and industrial emulsions in aqueous solvents.
• Integrated plasma cleaner
• Temperature controlled (4 degrees C and ambient).
• Typical sample volume 1 µL for 12 clipped grids.
• Biosafety laboratory level 2.

Linkam-Zeiss correlative fluorescence light microscopy for vitrified specimens.

• For detection of fluorescence in vitrified specimens prior to EM. The region of interest can be rapidly located and then used for intance in electron tomography.

FEI TALOS Artica transmission electron microscope equipped with a Falcon 4i direct electron detector camera and FEI phase plate.

• FEI TALOS Arctica transmission electron microscope with an advanced Falcon 4i camera, a phase plate, Fringe-Free Imaging and the Aberration Free Imaging System.
• Improved signal-to-noise ratio, greater sensitivity and automated data collection (24/7) enabling high resolution cryo-EM.
• Only system available in Finland.
• Advanced techniques available include correlative light and electron microscopy for vitrified specimens (CLEM).
• Data can be transferred to the CSC Ltd for processing of frames, or returned on a USB drive.

• CryoEM services are open to both academic and commercial users.
• Projects will undergo scientific review for their feasibility.

Instructions how to start a new project:

1. Contact the staff (grp-cryoemservice(at)helsinki.fi).
2. Have a kickoff meeting.
3. Once sample delivery has been agreed, fill in the CryoEM project form in iLAB.
4. https://hilife-infra.ilab.agilent.com/service_center/show_external/3753/instruc…
5. Samples are brought to Biocenter 1, EM unit floor and delivered to Kiran Ahmad Or Tuomas Niemi-Aro at an agreed date and time.
6. Samples are made and images are collected and delivered to the customer.

Instruct-ERIC access

Finland is member of Instruct-ERIC that provides open access to research infrastructure in structural biology. Helsinki cryoEM services is one of the service providers.

Services are available to academic and industry researchers from all countries, but researchers from member countries can apply for funding. The funding can be applied for instrument use, consumables, travel and accommodation. For more information about Instruct-ERIC, please see Instruct-ERIC webpages.

ACKNOWLEDGEMENT

Please notice that by using cryoEM service academic customers commit to acknowledge the unit in their publications or theses.  Please remember to add following sentences in your publication. We highly appreciate it.

"We thank Kiran Ahmad and Tuomas Niemi-Aro (University of Helsinki) for technical assistance in cryoEM. The facilities and expertise of the HiLIFE CryoEM unit at the University of Helsinki, a member of Instruct-ERIC Centre Finland, FINStruct, and Biocenter Finland are gratefully acknowledged."

CryoEM services offers Instrument time on Talos Arctica and sample preparation services. 
For Internal users services are either with service or, for experienced users, self-service. For external users only full service option is available. 
All usage has to be agreed with the staff via grp-cryoemservice@helsinki.fi at least 24h before booking.

All prices are VAT-exclusive. Standard rate of VAT is 25.5%.
Internal Academic price is for University of Helsinki users only. Price for Biocenter Finland (BF) users is the academic price + VAT 25,5%.

Billing is three times a year.

Internal academic

Talos Arctica instrument time

Example: Work started at 1PM, continued overnight; 3h + 17h; 60 €+335 € 

Sample preparation

*Includes Quantifoil R1.2/1.3 300 mesh Cu grids. Other grid types such as lacey holey carbon film, quantifoil R1.2/1.3 300 mesh Cu with an ultrathin Carbon layer available on request

**Includes UltrAuFoil R2/2 200 mesh Au grids. Other grid types such as Au-flat 1.2/1.3 300 mesh Au and Quantifoil R2/2 Cu 300 mesh coated with graphene oxide available on request

Storage and book keeping of cryogrids is the customer’s responsibility. 

Sample sheet needs to be filled in for all samples/grids that are stored in CryoEM facilities or submitted to CryoEM service for imaging.

Consumables (subject to availability)

External

For external academic and commercial users. Full service only.
Please also consider funding via instruct-ERIC.
Prices without VAT.

Sample Preparation

*Includes Quantifoil R1.2/1.3 300 mesh Cu grids. Other grid types such as lacey holey carbon film, quantifoil R1.2/1.3 300 mesh Cu with an ultrathin Carbon layer available on request

**Includes UltrAuFoil R2/2 200 mesh Au grids. Other grid types such as Au-flat 1.2/1.3 300 mesh Au and Quantifoil R2/2 Cu 300 mesh coated with graphene oxide available on request

Data collection with Talos Arctica

*Data set of the sample is typically 50 - 150 images. Such a data set will give you general information about your sample such as purity, size distribution and concentration.
 

Personnel                                                                                                                                    91,36 €/h              

•  For data processing                             

Contact us:

• Sarah Butcher, Director
• Kiran Ahmad, Laboratory Technician
• Tuomas Niemi-Aro, Laboratory Engineer

Email: grp-cryoemservice[at]helsinki.fi
Phone: +358294159010, +358294159502
Location: Viikki campus, Biocenter 1, Viikinkaari 9, 00790, University of Helsinki

Useful links about cryoEM

• https://www.nature.com/articles/d41586-020-00341-9
• https://www.youtube.com/watch?v=Qq8DO-4BnIY
• https://www.thermofisher.com/fi/en/home/electron-microscopy/life-sciences/learning-center.html?cid=2021-ls-gl-oncology&utm_source=em-university&utm_medium=3rd-party&utm_campaign=2021-ls-gl-oncology
• https://www.thermofisher.com/fi/en/home/electron-microscopy/life-sciences/learning-center/cryo-em-university.html
• https://www.thermofisher.com/fi/en/home/electron-microscopy/life-sciences/learning-center/webinars.html

Recent publications

2024

• Tammaro, C., Plavec, Z., Myllymäki, L., Mitchell, C., Consalvi, S., Biava, M., Ciogli, A., Domanska, A., Leppilampi, V., Buckner, C., Manetto, S., Sciò, P., Coluccia, A., Laajala, M., Dondio, G. M., Bigogno, C., Marjomäki, V., Butcher, S. J., & Poce, G. (2024). SAR Analysis of Novel Coxsackie virus A9 Capsid Binders. Journal of medicinal chemistry, 67(19), 17144–17161. https://doi.org/10.1021/acs.jmedchem.4c00701 
• Anastasina, M., Füzik, T., Domanska, A., Pulkkinen, L. I. A., Šmerdová, L., Formanová, P. P., Straková, P., Nováček, J., Růžek, D., Plevka, P., & Butcher, S. J. (2024). The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation. Science advances, 10(27), eadl1888. https://doi.org/10.1126/sciadv.adl1888
• Hannula, L., Kuivanen, S., Lasham, J., Kant, R., Kareinen, L., Bogacheva, M., Strandin, T., Sironen, T., Hepojoki, J., Sharma, V., Saviranta, P., Kipar, A., Vapalahti, O., Huiskonen, J. T., & Rissanen, I. (2024). Nanobody engineering for SARS-CoV-2 neutralization and detection. Microbiology Spectrum, 12(4). https://doi.org/10.1128/spectrum.04199-22
• Shroff, S., Haapakoski, M., Tapio, K., Laajala, M., Leppänen, M., Plavec, Z., Haapala, A., Butcher, S., ihalainen, J., Toppari, J., & Marjomäki, V. (2024). Antiviral action of a functionalized plastic surface against human coronaviruses. Microbiology Spectrum. https://doi.org/10.1128/spectrum.03008-23
• Henderikx, R. JM., Mann, D., Domanska, A., Dong, J., Shahzad, S., Lak, B., Filopoulou, A., Ludig, D., Grininger, M., Momoh, J., Laanto, E., Oksanen, H. M., Bisikalo, K., Williams, P. A., Butcher, S., Peters, P. J., & Beulen, B. W. A. M. M. (2024). VitroJet: new features and case studies. Acta crystallographica. Section D, Structural biology, 80(4). DOI: 10.1107/S2059798324001852 
• Laulumaa, S., Kumpula, EP., Huiskonen, J.T., Varjosalo, M. (2024). Structure and interactions of the endogenous human Commander complex. Nat Struct Mol Biol (2024). https://doi.org/10.1038/s41594-024-01246-1
• Kleywegt, G. J., Adams, P. D., Butcher, S. J., Lawson, C., Rohou, A., Rosenthal, P. B., Subramaniam, S., Topf, M., Abbott, S., Baldwin, P. R., Berrisford, J. M., Bricogne, G., Choudhary, P., Croll, T. I., Danev, R., Ganesan, S. J., Grant, T., Gutmanas, A., Henderson, R., ... Velankar, S. (Accepted/In press). Community recommendations on cryoEM data archiving and validation. International Union of Crystallography.

2023

• Sah-Teli, S. K., Pinkas, M., Hynönen, M. J., Butcher, S. J., Wierenga, R. K., Novacek, J., & Venkatesan, R. (2023). Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial β-oxidation trifunctional enzymes. Structure (London, England : 1993), 31(7), 812–825.e6. https://doi.org/10.1016/j.str.2023.04.011
• Es-Haghi M, Neustroeva O, Chowdhury I, Laitinen P, Väänänen M-A, Korvenlaita N, Malm T, Turunen MP, Turunen TA. Construction of Fusion Protein for Enhanced Small RNA Loading to Extracellular Vesicles. Genes. 2023; 14(2):261. https://doi.org/10.3390/genes14020261
• Seitz, I., Saarinen, S., Kumpula, E. P., McNeale, D., Anaya-Plaza, E., Lampinen, V., Hytönen, V. P., Sainsbury, F., Cornelissen, J. J. L. M., Linko, V., Huiskonen, J. T., & Kostiainen, M. A. (2023). DNA-origami-directed virus capsid polymorphism. Nature Nanotechnology. Advance online publication. https://doi.org/10.1038/s41565-023-01443-x
• Mäkelä, A. R., Ugurlu, H., Hannula, L., Kant, R., Salminen, P., Fagerlund, R., Mäki, S., Haveri, A., Strandin, T., Kareinen, L., Hepojoki, J., Kuivanen, S., Levanov, L., Pasternack, A., Naves, R. A., Ritvos, O., Österlund, P., Sironen, T., Vapalahti, O., ... Saksela, K. (2023). Intranasal trimeric sherpabody inhibits SARS-CoV-2 including recent immunoevasive Omicron subvariants. Nature Communications, 14(1), Article 1637. https://doi.org/10.1038/s41467-023-37290-6
• Karki, S., Javanainen, M., Rehan, S., Tranter, D., Kellosalo, J., Huiskonen, J., Happonen, L. J., & Paavilainen, V. (2023). Molecular view of ER membrane remodeling by the Sec61/TRAP translocon. EMBO Reports, 24, Article e57910. https://doi.org/10.15252/embr.202357910
• Rehan, S., Tranter, D., Sharp, P. P. P., Craven, G. B. B., Lowe, E., Anderl, J. L. L., Muchamuel, T., Abrishami, V., Kuivanen, S., Wenzell, N. A. A., Jennings, A., Kalyanaraman, C., Strandin, T., Javanainen, M., Vapalahti, O., Jacobson, M. P. P., McMinn, D., Kirk, C. J., Huiskonen, J. T., ... Paavilainen, V. O. (2023). Signal peptide mimicry primes Sec61 for client-selective inhibition. Nature Chemical Biology, 19, 1054–1062. https://doi.org/10.1038/s41589-023-01326-1
• Selvaraj, M., Kokate, S. B., Reggiano, G., Kogan, K., Kotila, T., Kremneva, E., DiMaio, F., Lappalainen, P., & Huiskonen, J. T. (2023). Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms. Cell Reports, 42(1), Article 111900. https://doi.org/10.1016/j.celrep.2022.111900

2022

• Lauri IA Pulkkinen*, Sarah V Barrass*, Aušra Domanska, Anna K Överby, Maria Anastasina, Sarah J Butcher. 2022. Molecular Organisation of Tick-Borne Encephalitis Virus. Viruses 14(4):792. https://doi.org/10.3390/v14040792
• Zlatka Plavec, Aušra Domanska, Xiaonan Liu, Pia Laine, Lars Paulin, Markku Varjosalo, Petri Auvinen, Sharon G Wolf, Maria Anastasina, Sarah J Butcher. 2022. SARS-CoV-2 Production, Purification Methods and UV Inactivation for Proteomics and Structural Studies. Viruses. 2022 Sep 8;14(9):1989. doi: 10.3390/v14091989. PMID: 36146795; PMCID: PMC9505060
• Aušra Domanska*, Zlatka Plavec*, Visa Ruokolainen*, Benita Löflund, Varpu Marjomäki, Sarah J Butcher. 2022. Structural Studies Reveal that Endosomal Cations Promote Formation of Infectious Coxsackievirus A9 A-Particles, Facilitating RNA and VP4 Release. J.Virol.  2022 Nov 30:e0136722. doi: 10.1128/jvi.01367-22 
• Muniyandi Selvaraj, Shrikant B. Kokate, Gabriella Reggiano, Konstantin Kogan, Tommi Kotila, Elena Kremneva, Frank DiMaio, Pekka Lappalainen, Juha T. Huiskonen, Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms, Cell Reports, 2022, 111900, ISSN 2211-1247, https://doi.org/10.1016/j.celrep.2022.111900.
• Kotila T, Wioland H, Selvaraj M, Kogan K, Antenucci L, Jégou A, Huiskonen JT, Romet-Lemonne G, Lappalainen P. Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite. Nat Commun. 2022 Jun 15;13(1):3442. doi: 10.1038/s41467-022-31068-y. PMID: 35705539; PMCID: PMC9200798.
• Kejzar N, Laanto E, Rissanen I, Abrishami V, Selvaraj M, Moineau S, Ravantti J, Sundberg LR, Huiskonen JT. Cryo-EM structure of ssDNA bacteriophage ΦCjT23 provides insight into early virus evolution. Nat Commun. 2022 Dec 3;13(1):7478. doi: 10.1038/s41467-022-35123-6. PMID: 36463224; PMCID: PMC9719478.
• Liina Hannula, Suvi Kuivanen, Jonathan Lasham, Ravi Kant, Lauri Kareinen, Mariia Bogacheva, Tomas Strandin, Tarja Sironen, Vivek Sharma, Petri Saviranta, Anja Kipar, Olli Vapalahti, Juha T. Huiskonen and Ilona Rissanen. (2022) Nanobody engineering for SARS-CoV-2 neutralization and detection. bioRxiv. https://doi.org/10.1101/2022.09.14.507920
• Kelly JJ, Tranter D, Pardon E, Chi G, Kramer H, Happonen L, Knee KM, Janz JM, Steyaert J, Bulawa C, Paavilainen VO, Huiskonen JT, Yue WW. (2022) Snapshots of actin and tubulin folding inside the TRiC chaperonin. Nat Struct Mol Biol. 2022 Apr 21. doi: 10.1038/s41594-022-00755-1.

2021

• Flatt, J.W.,  Domanska, A., Seppälä, A.L., Butcher, S.J. (2021) Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. Commun Biol 4:250  https://doi.org/10.1038/s42003-021-01779-x

2020

• Barreiro, K., Dwivedi, O. P., Leparc, G., Rolser, M., Delic, D., Forsblom, C., Groop, P. H., Groop, L., Huber, T. B., Puhka, M., & Holthofer, H. (2020). Comparison of urinary extracellular vesicle isolation methods for transcriptomic biomarker research in diabetic kidney disease. Journal of extracellular vesicles, 10(2), e12038. https://doi.org/10.1002/jev2.12038
• Mamata Bhattarai, Fabio Valoppi, Sami-Pekka Hirvonen, Sami Hietala, Petri Kilpeläinen, Vladimir Aseyev, Kirsi S. Mikkonen (2020) Time-dependent self-association of spruce galactoglucomannans depends on pH and mechanical shearing. Food Hydrocolloids Volume 102. https://doi.org/10.1016/j.foodhyd.2019.105607.
• Heikki Saari,Tiia Turunen,Andres Lõhmus,Mikko Turunen,Matti Jalasvuori,Sarah J. Butcher,Seppo Ylä-Herttuala,Tapani Viitala,Vincenzo Cerullo,Pia R. M. Siljander &Marjo Yliperttula. (2020) Extracellular vesicles provide a capsid-free vector for oncolytic adenoviral DNA delivery.Journal of Extracellular Vesicles, 9:1, 1747206, https://doi.org/10.1080/20013078.2020.1747206

2019

• Abdelnabi, R., Geraets, J.A., Ma, Y, Mirabelli, C., Flatt, J.W. , Domanska, A., Delang, L., Jochmans, D., Jayaprakash, V.,  Sinha, B.N.,  Leyssen, P., Butcher, S.J., Neyts , J. (2019) A novel druggable interprotomer pocket in the capsid of rhino- and enteroviruses. PLoS Biology 17: e3000281. https://doi.org/10.1371/journal.pbio.3000281
• Domanska, A. Flatt, J.W., Jukonen, J.J.J., Geraets, J.A., Butcher, S.J.  (2019) 2.8 Å resolution cryo-EM structure of human parechovirus 3 in complex with Fab from a neutralizing antibody. J. Virol   93:e01597-18. doi: 10.1128/JVI.01597-18
• Pooch F, Sliepen M, Knudsen KD, Nyström B, Tenhu H, Winnik FM. (2019) Poly(2-isopropyl-2-oxazoline)-b-poly(lactide) (PiPOx-b-PLA) Nanoparticles in Water: Interblock van der Waals Attraction Opposes Amphiphilic Phase Separation. Macromolecules. 2019 Feb 12;52(3):1317-1326. doi: 10.1021/acs.macromol.8b02558. Epub 2019 Feb 1. PMID: 31496543
• Ruokolainen V., Domanska, A., Pellicia, M., Laajala, M., Butcher, S.J., Marjomäki, M. (2019) Extracellular albumin and endosomal ions prime enterovirus particles for uncoating that can be prevented by fatty acid saturation. J. Virol. 93:e01597-18  doi: 10.1128/JVI.01597-18 https://doi.org/10.1128/JVI.00599-19
• Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R. (2019) Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic β-oxidation trifunctional enzyme complexes. Biochem J. 2019 Jul 15;476(13):1975-1994. doi: 10.1042/BCJ20190314. PMID: 31235482

2018

• Yang, D., Viitasuo, M., Pooch, F., Tenhu, H., Hietala, S. (2018) Poly(N-acryloylglycinamide) microgels as nanocatalyst platform. Polymer Chemistry. 9:4 517-524 doi: 10.1039/c7py01950e
• Hepojoki J, Hepojoki S, Smura T, Szirovicza L, Dervas E, Prähauser B, Nufer L, Schraner EM, Vapalahti O, Kipar A, Hetzel U. (2018). Characterization of Haartman Institute snake virus-1 (HISV-1) and HISV-like viruses-The representatives of genus hartmanivirus, family Arenaviridae. PLoS Pathog. 14:e1007415.

2017

• 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.

2016

• 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
• 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.

2015

• 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
• 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

2014

• 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
• 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.

2013

• 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
• 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, 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

2012

• 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
• 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.
• 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
• 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.
• 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

2011

• 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
• 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
• 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.