Affiliation: University of Copenhagen
- The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity?Kjell Håkansson
August Krogh Institute, LCMF, Universitetsparken 13, DK 210 0, Oe, Copenhagen, Denmark
Int J Biol Macromol 30:273-7. 2002..According to this, the Ramachandran values reflect the orientation of one of the backbone amino group that stabilises the oxyanion intermediate of catalysis...
- Homology modeling of Na,K-ATPase: a putative third sodium binding site suggests a relay mechanism compatible with the electrogenic profile of Na+ translocationK O Håkansson
Biomembrane Center, August Krogh Institute, University of Copenhagen, Denmark
Ann N Y Acad Sci 986:163-7. 2003..This relay mechanism may therefore be compatible with the electrogenic profile of Na(+) translocation...
- The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolutionKjell O Hakansson
August Krogh Institute, Copenhagen University, Universitetsparken 13, DK 2100 OE, Copenhagen, Denmark
J Mol Biol 332:1175-82. 2003..The positions of key residues are discussed in relation to the pattern of hydrophobicity, charge and sequence conservation of the molecular surface. The structure of a hexahistidine tag binding to nickel ions is presented...
- The three-dimensional structure of catalase from Enterococcus faecalisKjell O Hakansson
August Krogh Institute, Copenhagen University, Universitetsparken 13, DK 2100 Kbh O, Denmark
Acta Crystallogr D Biol Crystallogr 60:1374-80. 2004..mirabilis. The solvent structure in the active site is identical in the four subunits but differs from that found in other catalases. The structural consequences of the Ramachandran outlier Ser196 are discussed...
- Crystallization of mutant forms of glutaredoxin Grx1p from yeastKjell O Hakansson
Institute of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen O, Denmark
Acta Crystallogr Sect F Struct Biol Cryst Commun 62:920-2. 2006..0 A (synchrotron radiation) and 2.7 A (rotating-anode generator), respectively. In contrast, rxYFP-Grx1p formed crystals at high pH in MgSO(4) which diffract synchrotron radiation to 2.7 A...
- Structure of glutaredoxin Grx1p C30S mutant from yeastKjell O Hakansson
Department of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen Ø, Denmark
Acta Crystallogr D Biol Crystallogr 63:288-94. 2007..Conserved residues are clustered on one side of the active site...