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Alternative catalytic residues in the active site of Esco acetyltransferases
Ajam, T., De, I., Petkau, N., Whelan, G., Pena, V., & Eichele, G. (2020). Alternative catalytic residues in the active site of Esco acetyltransferases. Scientific Reports, 10(1), 9828 (13 pp.). https://doi.org/10.1038/s41598-020-66795-z
Nanoparticle size distribution from inversion of wide angle X-ray total scattering data
Ferri, F., Bertolotti, F., Guagliardi, A., & Masciocchi, N. (2020). Nanoparticle size distribution from inversion of wide angle X-ray total scattering data. Scientific Reports, 10, 12759 (11 pp.). https://doi.org/10.1038/s41598-020-69371-7
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein
Welte, H., Zhou, T., Mihajlenko, X., Mayans, O., & Kovermann, M. (2020). What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. Scientific Reports, 10(1), 2640 (12 pp.). https://doi.org/10.1038/s41598-020-59446-w
Conformational changes in apolipoprotein N-acyltransferase (Lnt)
Wiseman, B., & Högbom, M. (2020). Conformational changes in apolipoprotein N-acyltransferase (Lnt). Scientific Reports, 10(1), 639 (11 pp.). https://doi.org/10.1038/s41598-020-57419-7
Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension
Chaikuad, A., Thangaratnarajah, C., von Delft, F., & Bullock, A. N. (2019). Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension. Scientific Reports, 9(1), 18351 (10 pp.). https://doi.org/10.1038/s41598-019-54830-7
Rigid fusions of designed helical repeat binding proteins efficiently protect a binding surface from crystal contacts
Ernst, P., Honegger, A., van der Valk, F., Ewald, C., Mittl, P. R. E., & Plückthun, A. (2019). Rigid fusions of designed helical repeat binding proteins efficiently protect a binding surface from crystal contacts. Scientific Reports, 9(1), 16162 (10 pp.). https://doi.org/10.1038/s41598-019-52121-9
Structural analysis of biological targets by host:guest crystal lattice engineering
Ernst, P., Plückthun, A., & Mittl, P. R. E. (2019). Structural analysis of biological targets by host:guest crystal lattice engineering. Scientific Reports, 9(1), 15199 (11 pp.). https://doi.org/10.1038/s41598-019-51017-y
Position 123 of halohydrin dehalogenase HheG plays an important role in stability, activity, and enantioselectivity
Solarczek, J., Klünemann, T., Brandt, F., Schrepfer, P., Wolter, M., Jacob, C. R., … Schallmey, A. (2019). Position 123 of halohydrin dehalogenase HheG plays an important role in stability, activity, and enantioselectivity. Scientific Reports, 9(1), 5106 (10 pp.). https://doi.org/10.1038/s41598-019-41498-2
Conformational states during vinculin unlocking differentially regulate focal adhesion properties
Chorev, D. S., Volberg, T., Livne, A., Eisenstein, M., Martins, B., Kam, Z., … Geiger, B. (2018). Conformational states during vinculin unlocking differentially regulate focal adhesion properties. Scientific Reports, 8(1), 2693 (14 pp.). https://doi.org/10.1038/s41598-018-21006-8
Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin
Debela, M., Magdolen, V., Skala, W., Elsässer, B., Schneider, E. L., Craik, C. S., … Goettig, P. (2018). Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin. Scientific Reports, 8(1), 10705 (15 pp.). https://doi.org/10.1038/s41598-018-29058-6
COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens
Gebauer, J. M., Köhler, A., Dietmar, H., Gompert, M., Neundorf, I., Zaucke, F., … Baumann, U. (2018). COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens. Scientific Reports, 8(1), 17187. https://doi.org/10.1038/s41598-018-35447-8
Structure of the replication regulator Sap1 reveals functionally important interfaces
Jørgensen, M. M., Ekundayo, B., Zaratiegui, M., Skriver, K., Thon, G., & Schalch, T. (2018). Structure of the replication regulator Sap1 reveals functionally important interfaces. Scientific Reports, 8(1), 10930 (9 pp.). https://doi.org/10.1038/s41598-018-29198-9
Acylated-acyl carrier protein stabilizes the <em>Pseudomonas aeruginosa</em> WaaP lipopolysaccharide heptose kinase
Kreamer, N. N. K., Chopra, R., Caughlan, R. E., Fabbro, D., Fang, E., Gee, P., … Uehara, T. (2018). Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase. Scientific Reports, 8(1), 14124 (12 pp.). https://doi.org/10.1038/s41598-018-32379-1
Structural characterisation of the catalytic domain of botulinum neurotoxin X - high activity and unique substrate specificity
Masuyer, G., Zhang, S., Barkho, S., Shen, Y., Henriksson, L., Košenina, S., … Stenmark, P. (2018). Structural characterisation of the catalytic domain of botulinum neurotoxin X - high activity and unique substrate specificity. Scientific Reports, 8(1), 4518 (10 pp.). https://doi.org/10.1038/s41598-018-22842-4
Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide
Napiórkowska, M., Boilevin, J., Darbre, T., Reymond, J. L., & Locher, K. P. (2018). Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide. Scientific Reports, 8(1), 16297 (9 pp.). https://doi.org/10.1038/s41598-018-34534-0
Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of <em>Staphylococcus aureus</em>
Nöldeke, E. R., Muckenfuss, L. M., Niemann, V., Müller, A., Störk, E., Zocher, G., … Stehle, T. (2018). Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus. Scientific Reports, 8(1), 12953 (15 pp.). https://doi.org/10.1038/s41598-018-31098-x
Understanding the indirect DNA read-out specificity of I-CreI meganuclease
Prieto, J., Redondo, P., López-Méndez, B., D'Abramo, M., Merino, N., Blanco, F. J., … Molina, R. (2018). Understanding the indirect DNA read-out specificity of I-CreI meganuclease. Scientific Reports, 8(1), 10286 (9 pp.). https://doi.org/10.1038/s41598-018-28599-0
Predicting binding free energies of PDE2 inhibitors. The difficulties of protein conformation
Pérez-Benito, L., Keränen, H., van Vlijmen, H., & Tresadern, G. (2018). Predicting binding free energies of PDE2 inhibitors. The difficulties of protein conformation. Scientific Reports, 8(1), 4883 (10 pp.). https://doi.org/10.1038/s41598-018-23039-5
Thermal stabilization of the deglycating enzyme Amadoriase I by rational design
Rigoldi, F., Donini, S., Giacomina, F., Sorana, F., Redaelli, A., Bandiera, T., … Gautieri, A. (2018). Thermal stabilization of the deglycating enzyme Amadoriase I by rational design. Scientific Reports, 8(1), 3042 (14 pp.). https://doi.org/10.1038/s41598-018-19991-x
Towards high throughput GPCR crystallography: In Meso soaking of Adenosine A2A Receptor crystals.
Rucktooa, P., Cheng, R. K. Y., Segala, E., Geng, T., Errey, J. C., Brown, G. A., … Doré, A. S. (2018). Towards high throughput GPCR crystallography: In Meso soaking of Adenosine A2A Receptor crystals. Scientific Reports, 8(1), 41. https://doi.org/10.1038/s41598-017-18570-w