Dr. Todd Larsen & Professor George Reed, University of Wisconsin, Dr. Matthew Benning and Dr. Cary Bauer, Bruker AXS, Madison (USA)

Atomic Resolution Enolase data set at 1.10 Å

Dr. Matthew Benning, Bruker AXS Application Laboratory, Madison (USA)

Proteinase K from Tritirachium Album Limber at 0.95 Å Resolution.

Dr. Qingjun Ma, University of Göttingen (Germany)

Thaumatin 1.05Å test structure

Map after anisotropic model refinement

Dr. Cary Bauer and Dr. Matthew Benning, Bruker AXS Application Laboratory, Madison (USA)

Atomic Resolution data on Lysozym

mFo-Fc map contoured at 2.5σ

Prof. X.D. Su, Peking University, Beijing (China)

Crystal structure of human adenylate kinase 6

Refinement done on 2.0 Å measured in the home lab; Sulfur-SAD phasing done on 3Å data

Dr. Judit Eva Debreczeni, University of Göttingen (Germany)

Lima Beam Trypsin Inhibitor

Mol Wt: 7 KdA

Anomalous Scatters: 7 S-S

Space group: I213

Data resolution: 3.0 Å

Debreczeni et al., Acta Cryst,

D59, 393 (2003)

Dr. Judit Eva Debreczeni, University of Göttingen (Germany)

Viscotoxin A3

No. of aa: 46

Mol/asu: 1

Anomalous Scatters: 3 S-S

Data resolution: 2.2 Å

Debreczeni et al., Acta Cryst,

D59, 2125 (2003)

Dr. James Thoden & Prof. Hazel Holden, University of Wisconsin, Madison (USA)

UDP-Galactose 4-Epimerase from yeast at 1.85 Å

Dr. Tom Smith, Donald Danforth Plant Science Center, St. Luis (USA)

ZnuA periplasmic zinc binding component from Synechocystis

Goal: study metal specificity to make transgenic plants with altered metal absorption properties eg higher Zn content, or change to Pb, Cd…

42 kDa protein, high quality structure done completely in lab – 44,193 reflections, 1.8 Å resolution, 98% complete, Rsym 5.8%, Rmodel 21%

Dr. Tom Smith, Danforth Plant Science Center Symposium, Feb. 26, 2004

Copper radiation in-lab structure of antipsychotic drug sulpiride co-crystallized with human carbonic anhydrase isozyme II

P21, a=42.18, b=41.38, c=72.09, beta =104.4

180 secs/degree, 2 fold redundant, Rsym=4.79%, isomorphous structure refined to 1.6 Å resolution, verifying presence of inhibitor bound within the active site

Data quality allowed interactions between sulpiride & carbonic anhydrase to be investigated

Abbate, Coetzee, Casini, Ciattini, Scozzafava, Supuran, Bioorg. Med. Chem. Lett. 2004; 14:337

Dr. Andrea Hadfield, Department of Biochemistry, University of Bristol (UK)

Lactate captured in the active site of lactate dehydrogenase, 1.7Å data.

GCMBE at the Instituto de Química-Física Rocasolano, CSIC, Madrid (Spain)

Structural insights into the lipase/esterase behavior in the Candida rugosa lipase family: crystal structure of the lipase 2 isoenzyme at 1.97 Å resolution.

Prof. Yu Luo, University of Saskatchewan (Canada)

MR structure from homolog with 45% sequence identity

Crystal size 0.2x0.2x0.4 mm

2.0 Å lab data

Solved solely from lab source

Dr. J.L. Vanhooke and Professor H.F. Deluca, University of Wisconsin, Madison (USA)

Molecular structure of the rat vitamin D receptor ligand binding domain complexed with 2-carbon-substituted vitamin D3 hormone analogues and a LXXLL-containing coactivator peptide.

J.L. Vanhooke, M.M Benning, C.B. Bauer, J.W. Pike, H.F. Deluca. Biochemistry, 43(14), 2004.

E.A. Sickmier & C.L. Kielkopf, Johns Hopkins University, Baltimore (USA)

U2 Auxiliary Factor in complex with poly-uridine RNA oligonucleotide

“Crystal diffracts poorly & would have required synchrotron data if not for high brilliance microfocus generator” Prof. Clara Kielkopf, Johns Hopkins University

Y. Lin & C.L. Kielkopf, Johns Hopkins University, Baltimore (USA)

RNA oligonucleotide with adenosine bulge, containing the U2 snRNA/pre-mRNA Branch Point consensus sequences for RNA splicing

Structure by molecular replacement using native data from in-house X8 PROTEUM

S.Ni, et al., Chiron Corporation, Emeryville (USA)

Structure by molecular replacement using 2.0Å native data on in-house X8 PROTEUM

S.Ni, H.Robinson, G.Marsing, Dirksen S. Bussiere (Chiron), Michael A. Kennedy, Pacific Northwest National Lab, Acta Cryst D60 (2004)

Prof. G. W. Phillips Jr. et al, Center for Eukaryotic Structural Genomics (CESG), University of Wisconsin, Madison (USA)

“Our in-house Bruker AXS system used routinely for past year to screen new protein crystals for diffraction and development of cryoconditions for the CESG pipeline. To date ~20 new eukaryotic proteins have been solved & deposited in the PDB using the Bruker instrument.”

1XJ5 (top) and 1XYG (bottom)

Lopper, M., Holton, J. M., Keck, J. L.

Crystal Structure of Prib, a Component of the Escherichia Coli Replication Restart Primosome

Structure 12 pp. 1967 (2004)

Dr. H. Blanchard and Prof. M. von Itzstein, Institute for Glycomics, Griffith University (Australia)

Crystal structure of a rotavirus sialic-acid binding protein involved in the recognition of host-cell carbohydrates  that is critical to enabling virus-cell attachment and facilitating infection.

Timothy Cordes and Katrina Forest, Department of Bacteriology, University of Wisconsin, Madison (USA)

The structure of a homologue of the dimeric transcription factor Catabolite Repressor Protein has been refined at 2.7 Å resolution.

Each asymmetric unit of the I41 space group contains a single monomer bound to two cAMP molecules.