Jean Jeener NMR Centre

Established in 2010, the Jean Jeener NMR Centre houses state-of-the-art 600 MHz and 800 MHz NMR spectrometers dedicated to structural biology work. In addition to the main focus on biomolecular NMR projects of the Structural Biology Research Centre and other VIB departments, the NMR centre provides service to third-party academic and indutrial users. A range of service options (including spectrometer time, assistance with the experimental setup, and advanced spectral analysis) are available. Contact us for more details and pricing information.

The Jean Jeener NMR Centre is managed by Dr. Alex Volkov. See below for a description of our NMR spectrometers, the NMR Centre's research output, and follow us on Twitter (@BioNMRbe).


May 2017 Paper on the CBP ID3 - ZFP interaction by PRE NMR accepted in Sci. Rep. Congratulations to Sara Contreras-Martos!
Jun 2017 Bruker SampleCase sample changer (24 positions, temperature-controlled) installed on the 800 MHz spectrometer
Oct 2017 First in-house NMR-based screening is performed on 1,000 Ro3-compliant fragment library binding to a protein target
Aug 2018 Solution structure of the sushi 1 domain of GABABR1a is solved
Oct 2018 Solution structure of the YdaS transcription factor is solved by conjoint NOE-SAXS refinement
Nov 2018 The APP-GABABR1a story is out in Science. Congratulations to Heather Rice, Joris de Wit and other co-authors!
Sep 2019 Solution structure of the MsrB from C. diphtheriae is solved
Jan 2020 C. diphtheriae MsrB story is out in J.Biol.Chem. Congratulations to Maria-Armineh Tossounian!
Mar 2020 Solution structure of MiP from Pseudomonas bacteriophage is solved
Jan 2021 Solution structure of PaaR2 is solved
Apr 2021 The Cc-Erv1 story is out in J.Mol.Biol. Congratulations to Jan Riemer and Esra Peker!
Jul 2021 First in-house structure of a small molecule natural product elucidated
Mar 2022 P. aeruginosa diazetidomonapyridone story is out in J.Am.Chem.Soc. Congratulations to Steffen Drees and Ulrich Hennecke!
Oct 2022 NMR-guided directed evolution story is out in Nature. Congratulations to Korendovych lab!


600 MHz Varian (Agilent)

  • Four-channel (1H, 13C, 15N, 2H) spectrometer
  • Direct Drive 2 console
  • 1H(13C/15N) 5 mm PFG triple-resonance 13C-enhanced cold probe
  • Automatic tuning and matching
  • VnmrJ 4.1
800 MHz Varian/Bruker system

  • Four-channel (1H, 13C, 15N, 2H) spectrometer
  • Two reciever channels
  • AVIII HDX 800 console
  • Inverse triple-resonance H-C/N-D-05 Z TCI 5mm cryoprobe
  • Inverse triple-resonance H-C/N-D-05 Z TXI 5mm RT probe
  • Bruker Cooled SampleCase sample changer (24 positions)
  • TopSpin 3.6

Research Output

Research papers with contribution from the Jean Jeener NMR Centre

44.  Haufroid, M., Volkov, A.N. & Wouters, J. Targeting the phosphoserine phosphatase MtSerB2 for tuberculosis drug discovery, an hybrid knowledge based /fragment based approach. (2022) Eur. J. Med. Chem., in press.
43. Bhattacharya, S., Margheritis, E.G., Takahashi, K., Kulesha, A., D'Souza, A., Kim, I., Tame, J., Yoon, J.H,, Volkov, A.N., Makhlynets, O.V. & Korendovych, I.V. NMR-guided directed evolution. Nature 610, 389-93 (2022)..
42.  Ernst, S., Volkov, A.N., Stark, M., Hölscher, L., Steinert, K., Fetzner, S., Hennecke, U. & Drees, L.S. Azetidomonamide and diazetidomonapyridone metabolites control biofilm formation and pigment synthesis in Pseudomonas aeruginosa. J. Am. Chem. Soc. 144, 7676-85 (2022).
41.  Ben Bdira, F., Erkelens, A., Qin, L., Volkov, A.N.,  Andrew, L., Bowring, N., Boyle, A., Ubbink, M., Dove, S. & Dame, R.  Novel anti-repression mechanism of H-NS proteins by a phage protein.  Nucleic Acids Res. 49, 10770-84 (2021).
40.  Peker, E., Erdogan, A.J., Volkov, A.N. & Riemer, J. Erv1 and cytochrome c mediate rapid electron transfer via a collision-type interaction. J. Mol. Biol. 433, 167045 (2021).
39.  Ben Bdira, F., Waudby, C.A., Volkov, A.N., Schröder, S.P., AB, E., Codée, J.D.C., Overkleeft, H.S., Aerts, J.M.F.G., van Ingen, H. & Ubbink. M. Dynamics of ligand binding to a rigid glycosidase. Angew. Chem. Int. Ed.. 59, 20508-14 (2020).
38.  Tossounian, M.A., Truong, A.C., Buts, L., Wahni, K., Mourenza, A., Leermakers, M., Vertommen, D., Mateos, L.M., Volkov, A.N. & Messens, J. Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade. J.Biol.Chem. 295, 3664-77 (2020).

37.  Prolič-Kalinšek, M., De Bruyn, P., Juréna, D., Van Melderen, L., Loris, R. & Volkov, A.N. 1H, 13C, and 15N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family. Biomol. NMR Assign. 14, 25-30 (2020).

36  Makhlynets, O., Yoon, J.H., Kulesha, A.V., Lengyel-Zhand, Z., Volkov, A.N., Rempillo, J.J., D’Souza, A., Costeas, C., Chester, C. & Caselle, E.R. Uno Ferro, a de novo designed protein, binds transition metals with high affinity and stabilizes semiquinone radical anion. Chem. Eur. J. 25, 15252-6 (2019).

35.  Caselle, E.A., Yoon, J.H., Bhattacharya, S., Rempillo, J.J.L., Lengyel, Z., D'Souza, A., Moroz, Y.S., Tolbert P.L., Volkov, A.N., Forconi, M., Castañeda, C.A., Makhlynets, O.V. & Korendovych, I.V. Kemp Eliminases of the AlleyCat Family Possess High Substrate Promiscuity. ChemCatChem 11, 1425-30 (2019).

34.  Rice, H.C., de Malmazet, D., Schreurs, A., Frere, S., Van Molle, I., Volkov, A.N., Creemers, E., Vertkin, I., Nys, J., Ranaivoson, F.M., Comoletti, D., Savas, J.N., Remaut, H., Balschun, D., Wierda, K.D., Slutsky, I., Farrow, K., De Strooper, B. & de Wit, J. Secreted Amyloid-β Precursor Protein Functions as a GABABR1a Ligand to Modulate Synaptic Transmission. Science 363, eaao4827 (2019).

33.  Nguyen, H.H., Volkov, A.N., Vandenbussche, G., Tompa, P. & Pauwels, K. (2018) In vivo biotinylated calpastatin improves the affinity purification of human m-calpain. Prot. Expr. Purif. 145, 77-84.

32.  Kieken, F., Loth, K., van Nuland, N., Tompa, P. & Lenaerts, T. (2018) Chemical shift assignment of the partially deuterated Fyn SH2-SH3 domain. Biomol. NMR Assign. 12, 117-22.

31.  Contreras-Martos, S., Piai, A., Kosol, S., Varadi, M., Bekesi, A., Lebrun, P., Volkov, A.N., Gevaert, K., Pierattelli, R., Felli, I. & Tompa, P. (2017) Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. Sci. Rep. 7, 4676.

30. Huculeci, R., Cilia, E., Lyczek, A., Buts, L., Houben, K., Seeliger M.A., van Nuland, N.A.J. & Lenaerts, T. (2016) Dynamically coupled residues within the SH2 domain of FYN are key to unlocking its activity. Structure. 24, 1947-59.

29. Hubin, E., Cioffi, F., Rozenski, J., van Nuland, N.A.J. & Broersen, K. (2016) Characterization of insulin-degrading enzyme-mediated cleavage of Aß in distinct aggregation states. Biochim. Biophys, Acta 1860, 1281-90.

28. Antonik, P.M., Volkov, A.N., Broder, U.N., Lo Re, D., van Nuland, N.A.J. & Crowley, P.B. (2016) Anomer-specific recognition and dynamics in a fucose-binding lectin. Biochemistry 55, 1195-203.

27. Moroz, Y.S., Dunston, T.T., Makhlynets, O.V., Moroz, O.V., Wu, Y., Yoon, J.H., Olsen, A.B., McLaughlin, J.M., Mack, K.L., Gosavi, P.M., van Nuland, N.A.J. & Korendovych, I.V. (2015) New tricks for old proteins: single mutations in a nonenzymatic protein give rise to various enzymatic activities. J. Am. Chem. Soc. 137, 14905-11.

26. Huculeci, R., Garcia-Pino, A., Buts, L., Lenaerts, T. & van Nuland, N.A.J. (2015) Structural insights into the intertwined dimer of fyn SH2. Protein Sci. 24, 1964-78.

25. Van de Water, K., Sterckx, Y.G.J. & Volkov, A.N. (2015) The low-affinity complex of cytochrome c and its peroxidase. Nat. Commun. 6, 7073.

24. Zorzini, V., Buts, L., Schrank, E., Sterckx, Y.G.J., Respondek, M., Engelberg-Kulka, H., Loris, R., Zangger, K. & van Nuland, N.A.J. (2015) Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding. Nucleic Acids Res. 43, 1241-58.

23. Van de Water, K., van Nuland, N.A.J & Volkov, A.N. (2014) Transient protein encounters characterized by paramagnetic NMR. Chem. Sci. 5, 4227-36.

22. Sterckx, Y.G.J. & Volkov, A.N. (2014) Cofactor-dependent structural and binding properties of yeast cytochrome c peroxidase. Biochemistry 53, 4526-36.

21. Sterckx, Y.G.J., Volkov, A.N., Vranken, W.F., Kragelj, J., Ringkjøbing-Jensen, M., Buts, L., Garcia-Pino, A., Jové, T., Van Melderen, L., Blackledge, M., van Nuland, N.A.J. & Loris, R. (2014) SAXS and NMR-derived conformational ensemble of the highly flexible antitoxin PaaA2. Structure 22, 854-65.

20. Zorzini, V., Buts, L., Sleutel, M., Garcia-Pino, A., Talavera, A., Haesaerts, S., De Greve, H., Cheung, A, van Nuland, N.A.J. & Loris, R. (2014) Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics. Nucleic Acids Res. 42, 6709-25.

19. Vanwetswinkel, S., Volkov, A.N., Sterckx, Y.G.J., Garcia-Pino, A., Buts, L., Vranken, W.F., Bouckaert, J., Roy, R., Wyns, L. & van Nuland, N.A.J. (2014) Study of the structural and dynamic effects in the FimH adhesin upon α-D-heptyl mannose binding. J. Med. Chem. 57, 1416-27.

18. Ceregido, M.A., Spínola Amilibia, M., Buts, L., Rivera-Torres, J., Garcia-Pino, A., Bravo, J. & van Nuland, N.A.J. (2014) The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability. J. Mol. Biol. 426, 674-90.

17. Rubio, L., Huculeci, R., Buts, L., Vanwetswinkel, S., Lenaerts, T. & van Nuland, N.A.J. (2014) 1H, 13C, and 15N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain. Biomol. NMR Assign. 8, 297-301.

16. De Gieter, S., Loris, R., van Nuland, N.A.J. & Garcia-Pino, A(2014) 1H, 13C, and 15N backbone and sidechain chemical shift assignments of the toxin Doc in the unbound state. Biomol. NMR Assign. 8, 145-8.

15. Castro-Roa, D., Garcia-Pino, A., De Gieter, S., van Nuland, N.A.J., Loris, R. & Zenkin, N. (2013) The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu. Nat. Chem. Biol. 9, 811-7.

14. Ortega Roldan, J.L., Casares, S., Ringkjøbing Jensen, M., Cárdenes, N., Bravo, J., Blackledge, M., Azuaga, A.I. & van Nuland, N.A.J. (2013) Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications. PLoS One 8, e73018.

13. Vanwetswinkel, S., van Nuland, N.A.J. & Volkov, A.N. (2013) Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase. J. Biomol. NMR 57, 21-6.

12. Ceregido, M.A., Garcia-Pino, A., Ortega-Roldan, J.L., Casares, S., López Mayorga, O., Bravo, J., van Nuland, N.A.J. & Azuaga, A.I. (2013) Multimeric and differential binding of CIN85/CD2AP with two atypical proline-rich sequences from CD2 and Cbl-b. FEBS J. 280, 3399-415.

11. Volkov, A.N. & van Nuland, N.A.J. (2013) Solution NMR study of the yeast cytochrome c peroxidase - cytochrome c interaction. J. Biomol. NMR 56, 255-63.

10. Volkov, A.N., Wohlkonig, A., Soror, S.H. & van Nuland, N.A.J. (2013) Expression, purification, characterization, and solution nuclear magnetic resonance study of highly deuterated yeast cytochrome c peroxidase with enhanced solubility. Biochemistry 52, 2165-75.

9. Shah, D.M., AB, E., Diercks, T., Hass, M.A.S., van Nuland, N.A.J. & Siegal, G.D. (2012) Rapid protein-ligand co-structures from sparse NOE data. J. Med. Chem. 55, 10786-90.

8. Van Laer, K., Buts, L., Foloppe, N., Vertommen, D., Van Belle, K., Wahni, K., Roos, G., Nilsson, L., Mateos, L.M., Rawat, M., van Nuland, N.A.J. & Messens, J. (2012) Mycoredoxin-1 is one of the missing links in the oxidative stress defense mechanism of Mycobacteria. Mol. Microbiol. 86, 787-804.

7. Volkov, A.N., Vanwetswinkel, S., Van de Water, K. & van Nuland, N.A.J. (2012) Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy. J. Biomol. NMR52, 245-56.

6. Abskharon, R.N., Ramboarina, S., El Hassan, H., Gad, W., Apostol, M.I., Giachin, G., Legname, G., Steyaert, J., Messens, J., Soror, S.H. & Wohlkonig, A. (2012) A novel expression system for production of soluble prion proteins in E. coli. Microb. Cell Fact. 11, 6.

5. Jensen, M.R., Ortega-Roldan, J.L., Salmon, L., van Nuland, N.A.J. & Blackledge, M. (2011) Characterizing weak protein-protein complexes by NMR residual dipolar couplings. Eur. Biophys. J. 40, 1371-81.

4. Ortega-Roldan, J.L., Blackledge, M., van Nuland, N.A.J. & Azuaga, A.I. (2011) Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2APJ. Biomol. NMR 50, 103-17.

3. Huculeci, R., Buts, L., Lenaerts, T. & van Nuland N.A.J. (2011) 1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide. Biomol. NMR Assign. 5, 181-4.

2. Zorzini, V., Haesaerts, S., Cheung, A., Loris, R. & van Nuland, N.A.J. (2011) 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase. Biomol. NMR Assign. 5, 157-60.

1. Garcia-Pino, A., Balasubramanian, S., Wyns, L., Gazit, E., De Greve, H., Magnuson, R.D., Charlier, D., van Nuland, N.A.J. & Loris R. (2010) Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. Cell 142, 101-11.