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Coauthors
Marta Hammerstad Department of Biosciences, University of Oslo, Norway
1 protocol

Marie Lofstad Department of Biosciences, University of Oslo, Norway
1 protocol

Ingvild Gudim Department of Biosciences, University of Oslo, Norway
1 protocol

Hans-Petter Hersleth
  • Department of Biosciences, University of Oslo, Norway
  • 1 Author merit

Education

Ph.D, Department of Chemistry, University of Oslo, Norway, 2007

Current position

Senior Lecturer/Principal Investigator, Department of Biosciences and Department of Chemistry, University of Oslo, Norway

Publications

  1. Lofstad, M., Gudim, I., Hammerstad, M., Rohr, A. K. and Hersleth, H. P. (2016). Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus. Biochemistry 55(36): 4998-5001.
  2. Skramo, S., Hersleth, H. P., Hammerstad, M., Andersson, K. K. and Rohr, A. K. (2014). Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus. Acta Crystallogr F Struct Biol Commun 70(Pt 6): 777-780.
  3. Hammerstad, M., Hersleth, H. P., Tomter, A. B., Rohr, A. K. and Andersson, K. K. (2014). Crystal structure of Bacillus cereus class Ib ribonucleotide reductase di-iron NrdF in complex with NrdI. ACS Chem Biol 9(2): 526-537.
  4. Rackwitz, S., Faus, I., Schmitz, M., Kelm, H., Krüger, H. J., Andersson, K. K., Hersleth, H. P., Achterhold, K., Schlage, K., Wille, H. C., Schünemann, V. and Wolny, J. A. (2014). A New Sample Enviroment for Cryogenic Nuclear Resonance Scattering experiments on Single Crystals and Microsamples at P01, PETRA III. Hyperfine Interactions 226: 673-678.
  5. Zhao, X., Hersleth, H. P., Zhu, J., Andersson, K. K. and Magliozzo, R. S. (2013). Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid. Chem Commun (Camb) 49(99): 11650-11652.
  6. Can, M., Krucinska, J., Zoppellaro, G., Andersen, N. H., Wedekind, J. E., Hersleth, H. P., Andersson, K. K. and Bren, K. L. (2013). Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure. Chembiochem 14(14): 1828-1838.
  7. Tomter, A. B., Zoppellaro, G., Andersen, N. H., Hersleth, H. P., Hammerstad, M., Røhr, Å. K., Sandvik, G. K., Strand, K. R., Nilsson, G. E., Bell III, C. B., Barra, A. L., Blasco, E., Le Pape, L., Solomon, E. I. and Andersson, K. K. (2013).  Ribonucleotide reductase class I with different radical generating clusters. Coord. Chem. Rev. 257(1): 3-26.
  8. Andersen, C. B., Torvund-Jensen, M., Nielsen, M. J., de Oliveira, C. L., Hersleth, H. P., Andersen, N. H., Pedersen, J. S., Andersen, G. R. and Moestrup, S. K. (2012). Structure of the haptoglobin-haemoglobin complex. Nature 489(7416): 456-459.
  9. Hersleth, H. P. and Andersson, K. K. (2011). How different oxidation states of crystalline myoglobin are influenced by X-rays. Biochim Biophys Acta 1814(6): 785-796.
  10. Rohr, A. K., Hersleth, H. P. and Andersson, K. K. (2010). Tracking flavin conformations in protein crystal structures with Raman spectroscopy and QM/MM calculations. Angew Chem Int Ed Engl 49(13): 2324-2327.
  11. Muffler, K., Wolny, J. A., Hersleth, H. P., Andersson, K. K., Achterhold, K., Rüffer, R. and Schünemann, V. (2010). Installation of an IR/Raman measuring station at the ESRF for simultaneous detection of vibrational and nuclear resonant scattering spectra. J. Phys.: Conf. Ser. 217: 012004, 4pp.
  12. Zoppellaro, G., Bren, K. L., Ensign, A. A., Harbitz, E., Kaur, R., Hersleth, H. P., Ryde, U., Hederstedt, L. and Andersson, K. K. (2009). Review: studies of ferric heme proteins with highly anisotropic/highly axial low spin (S = 1/2) electron paramagnetic resonance signals with bis-histidine and histidine-methionine axial iron coordination. Biopolymers 91(12): 1064-1082.
  13. Hersleth, H. P., Hsiao, Y. W., Ryde, U., Gorbitz, C. H. and Andersson, K. K. (2008). The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates. Chem Biodivers 5(10): 2067-2089.
  14. Hersleth, H. P., Hsiao, Y. W., Ryde, U., Gorbitz, C. H. and Andersson, K. K. (2008). The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection. Biochem J 412(2): 257-264.
  15. Hersleth, H. P., Varnier, A., Harbitz, E., Røhr, Å. K., Schmidt, P. P., Sørlie, M., Cederkvist, F. H., Marchal, S., Gorren, A. C. F., Mayer, B., Uchida, T., Schünemann, V., Kitagawa, T., Trautwein, A. X., Shimizu, T., Lange, R., Görbitz, C. H. and Andersson, K. K. (2008). Reactive complexes in myoglobin and nitric oxide synthase. Inorg. Chim. Acta 361(4): 831-843.
  16. Hersleth, H. P., Uchida, T., Rohr, A. K., Teschner, T., Schunemann, V., Kitagawa, T., Trautwein, A. X., Gorbitz, C. H. and Andersson, K. K. (2007). Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O. J Biol Chem 282(32): 23372-23386.
  17. Hersleth, H. P., Ryde, U., Rydberg, P., Gorbitz, C. H. and Andersson, K. K. (2006). Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases. J Inorg Biochem 100(4): 460-476.
  18. Nilsson, K., Hersleth, H. P., Rod, T. H., Andersson, K. K. and Ryde, U. (2004). The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement. Biophys J 87(5): 3437-3447.
  19. Hersleth, H. P., Dalhus, B., Gorbitz, C. H. and Andersson, K. K. (2002). An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2. J Biol Inorg Chem 7(3): 299-304.
  20. Gorbitz, C. H. and Hersleth, H. P. (2000). Selective solvent inclusion as a tool for mapping molecular properties in crystal structures: a diethylstilbestrol example. Acta Crystallogr B 56 ( Pt 6): 1094-1102.
  21. Gorbitz, C. H. and Hersleth, H. P. (2000). On the inclusion of solvent molecules in the crystal structures of organic compounds. Acta Crystallogr B 56 (Pt 3): 526-534.
1 Protocol published
Measurement of FNR-NrdI Interaction by Microscale Thermophoresis (MST)
Authors:  Ingvild Gudim, Marie Lofstad, Marta Hammerstad and Hans-Petter Hersleth, date: 04/20/2017, view: 1745, Q&A: 0
This protocol describes how to measure protein-protein interactions by microscale thermophoresis (MST) using the MonolithTM NT.115 instrument (NanoTemper). We have used the protocol to determine the binding affinities between three ...