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Kirscht A, Kaptan SS, Bienert GP, Chaumont F, Nissen P, de Groot BL, Kjellbom P, Gourdon P, Johanson U (2016) Crystal Structure of an Ammonia-Permeable Aquaporin. Plos Biol. 30;14(3):e1002411.


Aurelius O, Johansson R, Bågenholm V, Lundin D, Tholander F, Balhuizen A, Beck T, Sahlin M, Sjöberg BM, Mulliez E, Logan DT (2015) The crystal structure of Thermotoga maritima class III ribonucleotide reductase lacks a radical cysteine pre-positioned in the active site. PLoS One 10(7):e0128199.

Sprenger J, Svensson B, Hålander J, Carey J, Persson L & Al-Karadaghi S. (2015) Three-dimensional structures of Plasmodium falciparum spermidine synthase with bound inhibitors suggest new strategies for drug design. Acta Crystallogr. D. Biol. Crystallogr., 71, 484-93.

Badarau A, Rouha H, Malafa S, Logan DT, Håkansson M, Stulik L, Dolezilkova I, Teubenbacher A, Gross K, Maierhofer B, Weber S, Jägerhofer M, Hoffman D & Nagy E (2015) Structure-function analysis of heterodimer formation, oligomerization and receptor binding of the Staphylococcus aureus bi-component toxin LukGH. J. Biol. Chem. 290, 142-156, doi: 10.1074/jbc.M114.598110

Rodrigues T, Reker D, Welin M, Caldera M, Brunner C, Gabernet G, Schneider P, Walse B, Schneider G. (2015) De Novo Fragment Design for Drug Discovery and Chemical Biology. Angew Chem Int Ed Engl. 54, 15079-15083. doi: 10.1002/anie.201508055.

Kim JE, Son JE, Jeong H, Kim DJ, Seo SG, Lee E, Lim TG, Kim JR, Kimbung YR, Chen H, Bode AM, Lee KW, Dong Z. (2015) A Novel Cinnamon-Related Natural Product with Pim-1 Inhibitory Activity Inhibits Leukemia and Skin Cancer. Cancer Res. 75, 2716-28. doi: 10.1158/0008-5472.CAN-14-3655.


Wisniewska M, Happonen L, Varjosala V, Malmström L, Rosenberger J, Pozdnyakova I, Frick IM, Björck L, Streicher W, Malmström J, Wikström M (2014) Functional and structural properties of a novel protein and virulence factor (protein sHIP) in Streptococcus pyogenes. J. Biol. Chem. 289, 18175-18188

von Schantz L, Håkansson M, Logan DT, Nordberg Karlsson E & Ohlin M (2014) Polar interactions with branching xyloses and CH-π interactions define carbohydrate binding module recognition of xyloglucan. Proteins 82, 3466-3475. doi: 10.1002/prot.24700


Danielsson J, Awad W, Saraboji K, Kurnik M, Lang L, Leinartaité L, Marklund SL, Logan DT & Oliveberg M (2013) Global structural motions from the strain of a single hydrogen bond. Proc. Natl. Acad. Sci. USA 110, 3829–34

Ejby M, Vujicic-Zagar A, Fredslund F,  Svensson B, Slotbom DJ, Abu Hachem M (2013) Structural basis for arabinoxylo-oligosaccharide capture by the probiotic Bifidobacterium animalis subsp. lactis Bl-04. Mol. Microbiol. 90, 1100–12

Singh B, al-Jubair T, Thunnissen MMGM, Mörgelin M & Riesbeck K (2013) The unique structure of Haemophilus influenzae protein E reveals multiple binding sites for host factors. Infect. Immun. 81, 801-814.


E. Haglund, J. Danielsson, S. Kadhirvel, M.O. Lindberg, D.T. Logan and M. Oliveberg (2012)  Trimming down a protein to its bare foldons. J. Biol. Chem. 287, 2731–8

M.S. Humble, K.E. Cassimjee, M. Håkansson, Y.R. Kimbung, B. Walse, V. Abedi, H-J Federsel, P. Berglund and D.T. Logan (2012) Crystal structure of the Chromobacterium violaceum omega-transaminase reveal major structural rearrangements upon binding of coenzyme PLP. FEBS J. 279, 779–92

Saraboji K., M. Håkansson, S. Genheden, C. Diehl, J, Qvist, U. Weininger, U.J. Nilsson, H. Leffler, U. Ryde, M. Akke and D.T. Logan (2012) The carbohydrate-binding site in galectin-3 is preorganized to recognize a sugarlike framework of oxygens: ultra-high-resolution structures and water dynamics. Biochemistry 51, 296–306

L. von Schantz, M. Håkansson, D.T. Logan, B. Walse, J. Österlin, E. Nordberg-Karlsson and M. Ohlin (2012) Structural basis for carbohydrate-binding specificity - a comparative assesment of two engineered carbohydrate-binding modules. Glycobiology 22, 948–61

B. Singh, T. Al Jubair, K. Förnvik, M.M. Thunnissen and K. Riesbeck (2012) Crystallisation and X-ray diffraction analysis of a novel surface-adhesin protein: protein E from Haemophilus influenzae. Acta Crystallogr. F 68, 222–6

G. Svensson, W. Awad, M. Håkansson, K. Mani and D.T. Logan (2012) Crystal structure of N-glycosylated human glypican-1 core protein. J. Biol. Chem. 287, 14040-51


C. Helgstrand, M. Hasan, H. Uysal, J.Z. Häggström, M.M. Thunnissen (2011) A leukotriene A4 hydrolase-related aminopeptidase from yeast undergoes induced fit upon inhibitor binding. J. Mol. Biol. 406, 120-34


C. Diehl, O. Engström, T. Delaine, M. Håkansson, S. Genheden, K. Modig, H. Leffler, U. Ryde, U. J. Nilsson, and M. Akke (2010). Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3. J. Am. Chem. Soc. 132, 14577-89

R. Johansson, E. Torrents, D. Lundin, J. Sprenger, M. Sahlin, B-M. Sjöberg and D. T. Logan (2010) High-resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states - an unusual flavodoxin. FEBS J 277, 4265-4277.

L. Leinartaité, K. Saraboji, A. Nordlund, D. T. Logan, and M. Oliveberg (2010). Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1. J. Am. Chem. Soc. 132, 13495-13504.

Pozzo T, Linares-Pasten J, Nordberg Karlsson E & Logan DT (2010) Structural and functional analyses of β-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3. J. Mol. Biol. 397, 724-739.


A. Nordlund, L. Leinartaité, K. Saraboji, C. Aisenbrey, G. Gröbner, J. Danielsson, D.T. Logan, and M. Oliveberg (2009) Functional features cause misfolding of the ALS-provoking enzyme SOD1: non-native metal coordination obstructs active-site packing. Proc. Natl. Acad. Sci. U.S.A, 106, 9667-9672

Redzynia I, Ljunggren A, Bujacz AD, Abrahamson M, Jaskolski M, Bujacz G (2009) Crystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteases. FEBS J 276, 793-806


 Redzynia I, Ljunggren A, Abrahamson M, Mort JS, Krupa JC, Jaskolski M, Bujacz G (2008) Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B. J Biol Chem 283, 22815-25

Wang, E., M. C. Bauer, A. Rogstam, S. Linse, D. T. Logan, and C. von Wachenfeldt (2008) Structure and functional properties of the Bacillus subtilis transcriptional repressor Rex. Mol Microbiol 69, 466-478


Ljunggren A, Redzynia I, Alvarez-Fernandez M, Abrahamson M, Mort JS, Krupa JC, Jaskolski M, Bujacz G (2007) Crystal structure of the parasite protease inhibitor chagasin in complex with a host target cysteine protease. J Mol Biol  371, 137-53

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The LP3 labs are located on floor 1 in Biology building A, Sölvegatan 35, Lund.

The Biology Building

Lund Protein Production Platform
Biology Building A
Sölvegatan 35

+46 46 2227785

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LP3 acknowledges generous financial support from Lund University, Knut and Alice Wallenberg Foundation (SWEGENE programme), the Erik & Maja Lundqvist Foundation, the Carl Tesdorpf Foundation and the Swedish Research Council.