List of publications


Archaea

Lindas, A.C., Chruszcz, M., Bernander, R. & Valegard, K.

Structure of creanactin, an archaeal actin homologue active at 90 C.

Acta Cryst. D70 (2014) 2126-2132.


Enzymes in the biosynthetic pathway of beta-lactams

Valegard, K., Terwisscha van Scheltinga, A.C., Lloyd, M.D., Hara, T., Ramaswamy, S., Perrakis, A., Thompson, A., Lee H-J., Baldwin, J.E., Schoefield, C.J., Hajdu, J. & Andersson, I.

Structure of a cephalosporin synthase.

Nature 394 (1998) 805-809.


Lloyd, M.D., Lee, H-J., Harlos, K., Zhang, Z-H., Baldwin, J.E., Schoefield, C.J., Charnock, J.M., Garner, C.D., Hara, T., Terwisscha van Scheltinga, A.C., Valegard, K., Viklund, J.A.C., Hajdu, J., Andersson, I., Danielsson, A. & Bhikhabhai, R.

Studies on the active site of deacetoxy-cephalosporin C synthase.

J. Mol. Biol. 287(1999) 943-960.


Terwisscha van Scheltinga, A.C., Valegard, K., Ramaswamy, S., Hajdu, J. & Andersson, I.

Multiple isomorphous replacement om merohedral twins: structure determination of deacetoxy-cephalosporin C synthase.

Acta Cryst. D57 (2001) 1776-1785.


Andersson, I., Terwisscha van Scheltinga, A.C. & Valegard, K.

Towards new beta-lactam antibiotics.

Cell. Mol. Life Sci. 58 (2001) 1897-1906.


Terwisscha van Scheltinga, A.C., Valegard, K., Hajdu, J. & Andersson, I.

MIR phasing using merohedrally twinned crystals.

Acta Cryst. D59 (2003) 2017-2022.


Valegard, K., Terwisscha van Scheltinga, A.C., Dubus, A., Ranghino, G., Oster, L.M., Hajdu, J. & Andersson, I.

The structural basis of cephalosporin formation in a mononuclear ferrous enzyme.

Nat. Struct. Biol. 11 (2004) 95-101.


Oster, L.M., Terwisscha van Scheltinga, A.C., Valegard, K., MacKenzie Hose, A., Dubus, A., Hajdu, J. & Andersson, I.

Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in a new crystal form of Deacetoxycephalosporin C synthase.

J. Mol. Biol. 343 (2004) 157-171.


Cicero, G., Carbonera, C.,Valegard, K., Hajdu, J. & Andersson, I.

Study of the oxidative half-reaction catalysed by a non-heme ferrous catalytic center by means of structural and computational methodologies.

Int. J. Quant. Chem. 107 (2004) 1514-1522.


Lejon,S. Ellis, J. & Valegard, K.

The last step in cephalosporin C formation revealed: Crystal structures of deacetylcephalosporin C acetyltransferase from Acremonium chrysogenum in complexes with reaction intermediates.

J. Mol. Biol. 377 (2008) 935-944.


MacKenzie A., Valegard, K., Iqbal, A., Caines, M.E.C., Kershaw, N., Schofield, C.J. & Andersson, I.

Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.

J. Mol. Biol. 396 (2010) 332-344.


Valegard, K., Iqbal, A., Kershaw, N., Ivison, D., Generaux, C., Dubus, A., Blikstad, C., Demetriades, M., Hopkinson, R.J., Lloyd, A.J., Roper, D.I., Schofield, C.J., Andersson. & McDonough, M-A.

Structural and mechanistic studies of the orf12 gene product from the clavulanic acid biosynthesis pathway

Acta Cryst. D69 (2013) 1567-1579.


Virus

Valegard, K., Unge, T., Montelius, I., Strandberg, B. & Fiers, W. Purificarion, crystallisation and preliminary X-ray data of the bacteriophage MS2.J. Mol. Biol. 190 (1986) 587-591.


Valegard, K., Liljas, L., Fridborg, K. & Unge, T. The three-dimensional structure of the bacterial virus MS2.Nature 345(1990) 36-41.


Valegard, K., Liljas, L., Fridborg, K. & Unge, T. Structure determination of the bacteriophage MS2.Acta Cryst. B47(1991) 949-960.


Golmohammadi, R., Valegard, K., Fridborg, K. & Liljas, L. The refined structure of bacteriophage MS2.J. Mol. Biol. 234(1993) 620-639.


Bundule, M., Pumpens, P., Ose, V., Valegard, K. & Liljas, L. Crystallisation of bacteriophage fr and its recombinant capsids.J. Mol. Biol. 232(1993) 1005-1006.


Stockley, P.G., Stonehouse, N.J. & Valegard, K. Molecular mechanism of RNA phage morphogenisis. Int. J. Biochem. 26(1994) 1249-1260.


Valegard, K., Fridborg, K. & Liljas, L. Crystallisation and preliminary X-ray diffraction studies of the bacteriophage Qb. Acta Cryst. D50(1994) 105-109.


Valegard, K., Murray, J. B., Stockley, P. G., Stonehouse, N. J. & Liljas, L. Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371(1994) 623-626.


Liljas, L., Fridborg, K., Valegard, K., Bundule, M. & Pumpens, P. Crystal structure of bacteriophage fr capsids at 3.5 A resolution. J. Mol. Biol. 244(1994) 279-290.


Stockley. P.G., Stonehouse, N. J., Murray, J.B., Goodman, S.T.S., Talbot, S.J., Adams, C.J., Liljas,L. & Valegard, K. Probing sequence-specific RNA recognition by the bacteriophage MS2 coat protein. Nucl.Acid.Res. 23(1995) 2512-2518.


Stonehouse, N. J., Valegard, K., Golmohammadi, R., van den Worm, S., Walton, C., Stockley, P.G. & Liljas, L. Crystal structures of MS2 capsids with mutations in the subunit FG loop. J. Mol. Biol. 256(1995) 330-339.


Golmohammadi, R., Fridborg, K., Bundule, M., Valegard, K. & Liljas, L. The crystal structure of the bacteriophage Qb at 3.5 A resolution. Structure 15(1996) 543-554.


Valegard, K., Murray, J. B., Stonehouse, N. J., van den Worm, S., Stockley, P.G. & Liljas, L. The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J. Mol. Biol. 270(1997) 724-738.


van den Worm, S., Stonehouse, N. J., Valegard, K., Murray, J. B., Walton, C., Fridborg, K., Stockley, P.G. & Liljas, L. Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments. Nucl. Acid Res. 26(1998) 1345-1351.


Grahn, E., Stonehouse, N. J., Murray, J. B., van den Worm, S., Valegard, K., Fridborg, K., Stockley, P.G. & Liljas, L. Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids: Implications for binding requirements. RNA 5(1998) 131-138.


Tito, M.A., Tars, K., Valegard, K., Hajdu, J. & Robinson, C.V. Electrospray time-of-flight mass spectometry of the intact MS2 virus capsid. J. Am. Chem. 122(2000) 3550.


Other enzymes

Dobson, R.C.J., Valegard, K. & Gerrard, J.A. The crystal structure of three site-directed mutants of Escherichia Coli dihydrodipicolinate synthase: Compelling evidence for a catalytic triad. J. Mol. Biol. 338(2004) 329-339.