Chair of Biochemistry

    Grimm, Clemens, Dr.

    Dr. Clemens Grimm

         +49 931 - 31 84031





    Curriculum vitae




    Clemens Grimm



    Laboratory Head, X-Ray Crystallography



    Chair of Biochemistry, Theodor-Boveri-Institute at the Biocentre
    University of Würzburg
    Am Hubland
    97074 Würzburg
    Phone +49 931 - 31 84031













    Studies in Biology, University of Frankfurt a. M., Germany



    Doctoral studies at the University of Marburg, Germany



    Postdoc at the University of Marburg, Germany



    Postdoc at the EMBL Grenoble, France


    since 2007

    Principal Investigator X-Ray Crystallography, Department of Biochemistry at the Biocenter, Würzburg, Germany






    Research Fields

    Structural characterization of RNP assembly complexes, LARP proteins






    1992-1998: Member of the German National Merit Foundation








    Original Manuscripts

    Grimm C, Chari A, Pelz JP, Kuper J, Kisker C, Diederichs K, Stark H, Schindelin H, Fischer U. Structural Basis of Assembly Chaperone- Mediated snRNP Formation. Mol Cell. (2013). Published online ahead of print.


    Pasternack SM, Refke M, Paknia E, Hennies HC, Franz T, Schäfer N, Fryer A, van Steensel M, Sweeney E, Just M, Grimm C, Kruse R, Ferrándiz C, Nöthen MM, Fischer U, Betz RC. (2012): Mutations in SNRPE, which Encodes a Core Protein of the Spliceosome, Cause Autosomal-Dominant Hypotrichosis Simplex. Am J Hum Genet. 92(1): 81-87.

    Grimm C, Chari A, Reuter K and Fischer U (2010): A crystallization screen based on alternative polymeric precipitants. Acta Crystallogr D Biol Crystallogr. 66: 685-697.

    Stirnimann CU, Ptchelkine D, Grimm C and Müller CW (2010): Structural basis of TBX5-DNA recognition: the T-box domain in its DNA-bound and -unbound form. J Mol Biol 400(1): 71-81.

    Grimm C, Matos R, Ly-Hartig N, Steuerwald U, Lindner D, Rybin V, Müller J and Müller CW (2009): Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt. Embo J 28(13): 1965-1977.

    Hames C, Ptchelkine D, Grimm C, Thevenon E, Moyroud E, Gerard F, Martiel JL, Benlloch R, Parcy F and Müller CW (2008): Structural basis for LEAFY floral switch function and similarity with helix-turn-helix proteins. Embo J 27(19): 2628-2637.

    Grimm C, de Ayala Alonso AG, Rybin V, Steuerwald U, Ly-Hartig N, Fischle W, Müller J and Müller CW (2007): Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg. EMBO Rep 8(11): 1031-1037.

    Grimm C, Ficner R, Sgraja T, Haebel P, Klebe G and Reuter K (2006): Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase. Biochem Biophys Res Commun 351(3): 695-701.

    Grimm C, Evers A, Brock M, Maerker C, Klebe G, Buckel W and Reuter K (2003): Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre. J Mol Biol 328(3): 609-621.

    Mamat B, Roth A, Grimm C, Ermler U, Tziatzios C, Schubert D, Thauer RK and Shima S (2002): Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship. Protein Sci 11(9): 2168-2178.

    Maser E, Xiong G, Grimm C, Ficner R and Reuter K (2001): 3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: biological significance, three-dimensional structure and gene regulation. Chem Biol Interact 130-132: 707-722.

    Grimm C, Maser E, Mobus E, Klebe G, Reuter K and Ficner R (2000): The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family. J Biol Chem 275(52): 41333-41339.

    Grimm C, Klebe G, Ficner R and Reuter K (2000): Screening orthologs as an important variable in crystallization: preliminary X-ray diffraction studies of the tRNA-modifying enzyme S-adenosyl-methionine:tRNA ribosyl transferase/isomerase. Acta Crystallogr D Biol Crystallogr 56(Pt 4): 484-488.