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Steiner Group


  • Steiner RA, Frerichs-Deeken, U, Fetzner, S (2007) Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily. Acta Crystallogr. F63, 382-385.
  • Valls, N, Steiner RA, Wright, G, Murshudov, GN, Subirana, JA (2005) Variable role of ions in two drug intercalation complexes of DNA. J. Biol. Inorg. Chem. 10, 476-482.
  • Vagin, AA, Steiner RA, Lebedev, AA, Potterton, L, McNicholas, S, Long, F, Murshudov GN (2004) REFMAC5 dictionary: organization of chemical prior knowledge and guidelines of its use. Acta Crystallogr. D60, 2184-2195.
  • Valls N, Wright, G, Steiner RA, Murshudov GN, Subirana, JA (2004) DNA variability in five crystal structures of d(CGCAATTGCG). Acta Crystallogr. D60, 680-685.
  • Steiner RA, Lebedev AA, Murshudov GN (2003) Fisher’s information in maximum-likelihood crystallographic refinement. Acta Crystallogr. D59, 2114-2124.
  • Fittipaldi M, Steiner RA, Matsushita M, Dijkstra BW, Groenen EJJ, Huber M. (2003) Single-crystal EPR study at 95 GHz of the type 2 copper site of the inhibitor-bound quercetin 2,3-dioxygenase. Biophysical J. 85, 4047-4054.
  • Steiner RA, Kalk KH, Dijkstra BW (2002) Anaerobic enzyme•substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA, 99, 16625-16630.
  • Steiner RA (2002) Mechanistic studies of the copper-dependent quercetin 2,3-dioxygenase from A. japonicus. X-ray crystallography, spectroscopy and theoretical calculations. Ph.D. thesis. University of Groningen.
  • Steiner RA, Meyer-Klaucke, W, Dijkstra BW (2002) Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin. Biochemistry, 41, 7963-7968.
  • Steiner RA, Kooter IM, Dijkstra BW (2002) Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights. Biochemistry, 41, 7955-7962.
  • Kooter IM*, Steiner RA*, Huber M, Dijkstra BW, van Noort PI, Egmond M (2002) - (*) equal contribution to the work EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates. Eur. J. Biochem. 269, 2971-2979.
  • Fusetti F*, Schroter KH*, Steiner RA, van Noort PI, Pijning T, Rozeboom HJ, Kalk K, Egmond MR, Dijkstra BW (2002)- (*) equal contribution to the work Crystal structure of the copper-containing quercetin 2,3-dioxygenase from A. japonicus. Structure, 10, 259-268.
  • Steiner RA, Rozeboom HJ, de Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra BW (2001) X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution. Acta Crystallogr. D57, 516-526.
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