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481 results on '"Garman, Elspeth F."'

2. Variability in X-ray induced effects in [Rh(COD)Cl]2 with changing experimental parameters

Author

Fernando, Nathalie K., Boström, Hanna L. B., Murray, Claire A., Owen, Robin L., Thompson, Amber L., Dickerson, Joshua L., Garman, Elspeth F., Cairns, Andrew B., and Regoutz, Anna

Subjects
Condensed Matter - Materials Science
Abstract

X-ray characterisation methods have undoubtedly enabled cutting-edge advances in all aspects of materials research. Despite the enormous breadth of information that can be extracted from these techniques, the challenge of radiation-induced sample change and damage remains prevalent. This is largely due to the emergence of modern, high-intensity X-ray source technologies and growing potential to carry out more complex, longer duration in-situ or in-operando studies. The tunability of synchrotron beamlines enables the routine application of photon energy-dependent experiments. This work explores the structural stability of [Rh(COD)Cl]2, a widely used catalyst and precursor in the chemical industry, across a range of beamline parameters that target X-ray energies of 8 keV, 15 keV, 18 keV and 25 keV, on a powder X-ray diffraction synchrotron beamline at room temperature. Structural changes are discussed with respect to absorbed X-ray dose at each experimental setting associated with the respective photon energy. In addition, the X-ray radiation hardness of the catalyst is discussed, by utilising the diffraction data at the different energies to determine a dose limit, which is often considered in protein crystallography and typically overlooked in small molecule crystallography. This work not only gives fundamental insight into how damage manifests in this organometallic catalyst, but will encourage careful consideration of experimental X-ray parameters before conducting diffraction on similar radiation-sensitive organometallic materials., Comment: 20 pages, 7 figures

Published
2022
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5. Insights into an unusual Auxiliary Activity 9 family member lacking the histidine brace motif of lytic polysaccharide monooxygenases

Author

Frandsen, Kristian EH, Tovborg, Morten, Jørgensen, Christian I, Spodsberg, Nikolaj, Rosso, Marie-Noëlle, Hemsworth, Glyn R, Garman, Elspeth F, Grime, Geoffrey W, Poulsen, Jens-Christian N, Batth, Tanveer S, Miyauchi, Shingo, Lipzen, Anna, Daum, Chris, Grigoriev, Igor V, Johansen, Katja S, Henrissat, Bernard, Berrin, Jean-Guy, and Lo Leggio, Leila

Subjects
Biochemistry and Cell Biology, Biological Sciences, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Histidine, Ligands, Mixed Function Oxygenases, Models, Molecular, Phosphorylation, Phylogeny, Polysaccharides, polysaccharide, copper monooxygenase, crystal structure, glycobiology, phosphorylation, biomass degradation, His-brace, N-terminal Arg-AA9, xylooligosaccharide, Chemical Sciences, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Chemical sciences
Abstract

Lytic polysaccharide monooxygenases (LPMOs) are redox-enzymes involved in biomass degradation. All characterized LPMOs possess an active site of two highly conserved histidine residues coordinating a copper ion (the histidine brace), which are essential for LPMO activity. However, some protein sequences that belong to the AA9 LPMO family display a natural N-terminal His to Arg substitution (Arg-AA9). These are found almost entirely in the phylogenetic fungal class Agaricomycetes, associated with wood decay, but no function has been demonstrated for any Arg-AA9. Through bioinformatics, transcriptomic, and proteomic analyses we present data, which suggest that Arg-AA9 proteins could have a hitherto unidentified role in fungal degradation of lignocellulosic biomass in conjunction with other secreted fungal enzymes. We present the first structure of an Arg-AA9, LsAA9B, a naturally occurring protein from Lentinus similis The LsAA9B structure reveals gross changes in the region equivalent to the canonical LPMO copper-binding site, whereas features implicated in carbohydrate binding in AA9 LPMOs have been maintained. We obtained a structure of LsAA9B with xylotetraose bound on the surface of the protein although with a considerably different binding mode compared with other AA9 complex structures. In addition, we have found indications of protein phosphorylation near the N-terminal Arg and the carbohydrate-binding site, for which the potential function is currently unknown. Our results are strong evidence that Arg-AA9s function markedly different from canonical AA9 LPMO, but nonetheless, may play a role in fungal conversion of lignocellulosic biomass.

Published
2019

8. Crystal structure of a bacterial photoactivated adenylate cyclase determined at room temperature by serial femtosecond crystallography

Author

Kapetanaki, Sofia M, primary, Coquelle, Nicolas, additional, von Stetten, David, additional, Byrdin, Martin, additional, Rios-Santacruz, Ronald, additional, Bean, Richard, additional, Bielecki, Johan, additional, Boudjelida, Mohamed, additional, Fekete, Zsuzsana, additional, Grime, Geoffrey W, additional, Han, Huijong, additional, Hatton, Caitlin, additional, Kantamneni, Sravya, additional, Kharitonov, Konstantin, additional, Kim, Chan, additional, Kloos, Marco, additional, Koua, Faisal H.M., additional, de Diego Martinez, Inaki, additional, Melo, Diogo, additional, Rane, Lukas, additional, Round, Adam, additional, Round, Ekaterina, additional, Sarma, Abhisakh, additional, Schubert, Robin, additional, Schulz, Joachim, additional, Sikorski, Marcin, additional, Vakili, Mohammad, additional, Valerio, Joana, additional, Vitas, Jovana, additional, de Wijn, Raphael, additional, Wrona, Agnieszka, additional, Zala, Ninon, additional, Pearson, Arwen, additional, Dorner, Katerina, additional, Schiro, Giorgio, additional, Garman, Elspeth F, additional, Lukacs, Andras, additional, and Weik, Martin, additional

Published
2024
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11. Doses for X‐ray and electron diffraction: New features in RADDOSE‐3D including intensity decay models.

Author

Dickerson, Joshua L., McCubbin, Patrick T. N., Brooks‐Bartlett, Jonathan C., and Garman, Elspeth F.

Abstract

New features in the dose estimation program RADDOSE‐3D are summarised. They include the facility to enter a diffraction intensity decay model which modifies the "Diffraction Weighted Dose" output from a "Fluence Weighted Dose" to a "Diffraction‐Decay Weighted Dose", a description of RADDOSE‐ED for use in electron diffraction experiments, where dose is historically quoted in electrons/Å2 rather than in gray (Gy), and finally the development of a RADDOSE‐3D GUI, enabling easy access to all the options available in the program. [ABSTRACT FROM AUTHOR]

Published
2024
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12. Identifying and avoiding radiation damage in macromolecular crystallography.

Author

Shelley, Kathryn L. and Garman, Elspeth F.

Subjects
*RADIATION damage, *CRYSTALLOGRAPHY
Abstract

Radiation damage remains one of the major impediments to accurate structure solution in macromolecular crystallography. The artefacts of radiation damage can manifest as structural changes that result in incorrect biological interpretations being drawn from a model, they can reduce the resolution to which data can be collected and they can even prevent structure solution entirely. In this article, we discuss how to identify and mitigate against the effects of radiation damage at each stage in the macromolecular crystal structure‐solution pipeline. [ABSTRACT FROM AUTHOR]

Published
2024
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15. The effect of irradiation-induced disorder on the conductivity and critical temperature of the organic superconductor $\kappa$-(BEDT-TTF)$_2$Cu(SCN)$_2$

Author

Analytis, James G., Ardavan, Arzhang, Blundell, Stephen J., Owen, Robin L., Garman, Elspeth F., Jeynes, Chris, and Powell, Ben J.

Subjects
Condensed Matter - Superconductivity
Abstract

We have introduced defects into clean samples of the organic superconductor $\kappa$-(BEDT-TTF)$_2$Cu(SCN)$_2$ in order to determine their effect on the temperature dependence of the conductivity and the critical temperature $T_{\rm c}$. We find a violation of Matthiessen's rule that can be explained by a model of the conductivity involving a defect-assisted interlayer channel which acts in parallel with the band-like conductivity. We observe an unusual dependence of $T_{\rm c}$ on residual resistivity which is not consistent with the generalised Abrikosov-Gor'kov theory for an order parameter with a single component, providing an important constraint on models of the superconductivity in this material.

Published
2005
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19. The CCP4 suite: integrative software for macromolecular crystallography

Author

Agirre, Jon, primary, Atanasova, Mihaela, additional, Bagdonas, Haroldas, additional, Ballard, Charles B., additional, Baslé, Arnaud, additional, Beilsten-Edmands, James, additional, Borges, Rafael J., additional, Brown, David G., additional, Burgos-Mármol, J. Javier, additional, Berrisford, John M., additional, Bond, Paul S., additional, Caballero, Iracema, additional, Catapano, Lucrezia, additional, Chojnowski, Grzegorz, additional, Cook, Atlanta G., additional, Cowtan, Kevin D., additional, Croll, Tristan I., additional, Debreczeni, Judit É., additional, Devenish, Nicholas E., additional, Dodson, Eleanor J., additional, Drevon, Tarik R., additional, Emsley, Paul, additional, Evans, Gwyndaf, additional, Evans, Phil R., additional, Fando, Maria, additional, Foadi, James, additional, Fuentes-Montero, Luis, additional, Garman, Elspeth F., additional, Gerstel, Markus, additional, Gildea, Richard J., additional, Hatti, Kaushik, additional, Hekkelman, Maarten L., additional, Heuser, Philipp, additional, Hoh, Soon Wen, additional, Hough, Michael A., additional, Jenkins, Huw T., additional, Jiménez, Elisabet, additional, Joosten, Robbie P., additional, Keegan, Ronan M., additional, Keep, Nicholas, additional, Krissinel, Eugene B., additional, Kolenko, Petr, additional, Kovalevskiy, Oleg, additional, Lamzin, Victor S., additional, Lawson, David M., additional, Lebedev, Andrey A., additional, Leslie, Andrew G. W., additional, Lohkamp, Bernhard, additional, Long, Fei, additional, Malý, Martin, additional, McCoy, Airlie J., additional, McNicholas, Stuart J., additional, Medina, Ana, additional, Millán, Claudia, additional, Murray, James W., additional, Murshudov, Garib N., additional, Nicholls, Robert A., additional, Noble, Martin E. M., additional, Oeffner, Robert, additional, Pannu, Navraj S., additional, Parkhurst, James M., additional, Pearce, Nicholas, additional, Pereira, Joana, additional, Perrakis, Anastassis, additional, Powell, Harold R., additional, Read, Randy J., additional, Rigden, Daniel J., additional, Rochira, William, additional, Sammito, Massimo, additional, Sánchez Rodríguez, Filomeno, additional, Sheldrick, George M., additional, Shelley, Kathryn L., additional, Simkovic, Felix, additional, Simpkin, Adam J., additional, Skubak, Pavol, additional, Sobolev, Egor, additional, Steiner, Roberto A., additional, Stevenson, Kyle, additional, Tews, Ivo, additional, Thomas, Jens M. H., additional, Thorn, Andrea, additional, Valls, Josep Triviño, additional, Uski, Ville, additional, Usón, Isabel, additional, Vagin, Alexei, additional, Velankar, Sameer, additional, Vollmar, Melanie, additional, Walden, Helen, additional, Waterman, David, additional, Wilson, Keith S., additional, Winn, Martyn D., additional, Winter, Graeme, additional, Wojdyr, Marcin, additional, and Yamashita, Keitaro, additional

Published
2023
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20. The Crystal Structure of the Escherichia coli RNase E Apoprotein and a Mechanism for RNA Degradation

Author

Koslover, Daniel J, Callaghan, Anastasia J, Marcaida, Maria J, Garman, Elspeth F, Martick, Monika, Scott, William G, and Luisi, Ben F

Subjects
Biochemistry and Cell Biology, Biological Sciences, Emerging Infectious Diseases, Genetics, Generic health relevance, Amino Acid Sequence, Apoproteins, Crystallography, X-Ray, Endoribonucleases, Escherichia coli, Escherichia coli Proteins, Molecular Sequence Data, Protein Structure, Quaternary, RNA, RNA Stability, Substrate Specificity, Chemical Sciences, Information and Computing Sciences, Biophysics, Biological sciences, Chemical sciences
Abstract

RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli. Here, we present the crystal structure of the E. coli RNase E catalytic domain in the apo-state at 3.3 A. This structure indicates that, upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site. The structural data suggest a mechanism of RNA recognition and cleavage that explains the enzyme's preference for substrates possessing a 5'-monophosphate and accounts for the protective effect of a triphosphate cap for most transcripts. Internal flexibility within the quaternary structure is also observed, a finding that has implications for recognition of structured RNA substrates and for the mechanism of internal entry for a subset of substrates that are cleaved without 5'-end requirements.

Published
2008

24. The CCP4 suite: integrative software for macromolecular crystallography

Author

Agirre, Jon, Atanasova, Mihaela, Bagdonas, Haroldas, Ballard, Charles B., Basle, Arnaud, Beilsten-Edmands, James, Borges, Rafael J., Brown, David G., Burgos-Marmol, J. Javier, Berrisford, John M., Bond, Paul S., Caballero, Iracema, Catapano, Lucrezia, Chojnowski, Grzegorz, Cook, Atlanta G., Cowtan, Kevin D., Croll, Tristan I., Debreczeni, Judit E., Devenish, Nicholas E., Dodson, Eleanor J., Drevon, Tarik R., Emsley, Paul, Evans, Gwyndaf, Evans, Phil R., Fando, Maria, Foadi, James, Fuentes-Montero, Luis, Garman, Elspeth F., Gerstel, Markus, Gildea, Richard J., Hatti, Kaushik, Hekkelman, Maarten L., Heuser, Philipp, Hoh, Soon Wen, Hough, Michael A., Jenkins, Huw T., Jimenez, Elisabet, Joosten, Robbie P., Keegan, Ronan M., Keep, Nicholas, Krissinel, Eugene B., Kolenko, Petr, Kovalevskiy, Oleg, Lamzin, Victor S., Lawson, David M., Lebedev, Andrey A., Leslie, Andrew G. W., Lohkamp, Bernhard, Long, Fei, Maly, Martin, McCoy, Airlie J., McNicholas, Stuart J., Medina, Ana, Millan, Claudia, Murray, James W., Murshudov, Garib N., Nicholls, Robert A., Noble, Martin E. M., Oeffner, Robert, Pannu, Navraj S., Parkhurst, James M., Pearce, Nicholas, Pereira, Joana, Perrakis, Anastassis, Powell, Harold R., Read, Randy J., Rigden, Daniel J., Rochira, William, Sammito, Massimo, Rodriguez, Filomeno Sanchez, Sheldrick, George M., Shelley, Kathryn L., Simkovic, Felix, Simpkin, Adam J., Skubak, Pavol, Sobolev, Egor, Steiner, Roberto A., Stevenson, Kyle, Tews, Ivo, Thomas, Jens M. H., Thorn, Andrea, Trivino Valls, Josep, Uski, Ville, Uson, Isabel, Vagin, Alexei, Velankar, Sameer, Vollmar, Melanie, Walden, Helen, Waterman, David, Wilson, Keith S., Winn, Martyn D., Winter, Graeme, Wojdyr, Marcin, Yamashita, Keitaro, Agirre, Jon, Atanasova, Mihaela, Bagdonas, Haroldas, Ballard, Charles B., Basle, Arnaud, Beilsten-Edmands, James, Borges, Rafael J., Brown, David G., Burgos-Marmol, J. Javier, Berrisford, John M., Bond, Paul S., Caballero, Iracema, Catapano, Lucrezia, Chojnowski, Grzegorz, Cook, Atlanta G., Cowtan, Kevin D., Croll, Tristan I., Debreczeni, Judit E., Devenish, Nicholas E., Dodson, Eleanor J., Drevon, Tarik R., Emsley, Paul, Evans, Gwyndaf, Evans, Phil R., Fando, Maria, Foadi, James, Fuentes-Montero, Luis, Garman, Elspeth F., Gerstel, Markus, Gildea, Richard J., Hatti, Kaushik, Hekkelman, Maarten L., Heuser, Philipp, Hoh, Soon Wen, Hough, Michael A., Jenkins, Huw T., Jimenez, Elisabet, Joosten, Robbie P., Keegan, Ronan M., Keep, Nicholas, Krissinel, Eugene B., Kolenko, Petr, Kovalevskiy, Oleg, Lamzin, Victor S., Lawson, David M., Lebedev, Andrey A., Leslie, Andrew G. W., Lohkamp, Bernhard, Long, Fei, Maly, Martin, McCoy, Airlie J., McNicholas, Stuart J., Medina, Ana, Millan, Claudia, Murray, James W., Murshudov, Garib N., Nicholls, Robert A., Noble, Martin E. M., Oeffner, Robert, Pannu, Navraj S., Parkhurst, James M., Pearce, Nicholas, Pereira, Joana, Perrakis, Anastassis, Powell, Harold R., Read, Randy J., Rigden, Daniel J., Rochira, William, Sammito, Massimo, Rodriguez, Filomeno Sanchez, Sheldrick, George M., Shelley, Kathryn L., Simkovic, Felix, Simpkin, Adam J., Skubak, Pavol, Sobolev, Egor, Steiner, Roberto A., Stevenson, Kyle, Tews, Ivo, Thomas, Jens M. H., Thorn, Andrea, Trivino Valls, Josep, Uski, Ville, Uson, Isabel, Vagin, Alexei, Velankar, Sameer, Vollmar, Melanie, Walden, Helen, Waterman, David, Wilson, Keith S., Winn, Martyn D., Winter, Graeme, Wojdyr, Marcin, and Yamashita, Keitaro

Abstract

The Collaborative Computational Project No. 4 (CCP4) is a UK-led international collective with a mission to develop, test, distribute and promote software for macromolecular crystallography. The CCP4 suite is a multiplatform collection of programs brought together by familiar execution routines, a set of common libraries and graphical interfaces. The CCP4 suite has experienced several considerable changes since its last reference article, involving new infrastructure, original programs and graphical interfaces. This article, which is intended as a general literature citation for the use of the CCP4 software suite in structure determination, will guide the reader through such transformations, offering a general overview of the new features and outlining future developments. As such, it aims to highlight the individual programs that comprise the suite and to provide the latest references to them for perusal by crystallographers around the world., Funding Agencies|Royal Society [UF160039, URF\R\221006, RGF/R1/181006]; UK Engineering and Physical Sciences Research Council (EPSRC) [EP/R513386/1]; BBSRC [BB/S007105/1, BB/S007083/1, BB/T012935/1, BB/S005099/1, BB/S007040/1]; European Union [871037]; CCP4; Medical Research Council as part of United Kingdom Research and Innovation; UK Research and Innovation: MRC [MC_UP_A025_1012]; European Molecular Biology Laboratory-European Bioinformatics Institute; German Federal Ministry of Education and Research [05K19WWA, 05K22GU5]; Deutsche Forschungsgemeinschaft [TH2135/2-1]; MEYS CR [CZ.02.1.01/0.0/0.0/16_019/0000778]; Czech Academy of Sciences [86652036]; CCP4/STFC [521862101]; iNEXT [653706]; iNEXT-Discovery [871037]; West-Life [675858]; EOSC-Life - Horizon 2020 program of the European Commission [824087]; Netherlands Organization for Scientific Research (NWO) [722.011.011, 723.013.003]; Dutch Cancer Society; Dutch Ministry of Health, Welfare and Sport; Wellcome Trust [209407/Z/17/Z]; Wellcome Trust SRF [200898]; Wellcome Centre for Cell Biology core grant [203149]; STFC-UK/CCP4: Agreement for the integration of methods into the CCP4 software distribution, ARCIMBOLDO_LOW; Spanish MICINN/AEI/FEDER/UE [PID2021-128751NB-I00]; NWOApplied Sciences and Engineering Domain; CCP4 [13337, 16219]; Rontgen Angstrom Cluster [349-2013-597]; SciLifeLab and Wallenberg Data Driven Life Science Program [KAW 2020.0239]; Dutch Research Council (NWO) [VI.Veni.192.143]; EMBO fellowship [ALTF 609-2017]; EPSRC [EP/G037280/1]; BBSRC Institute Strategic Programme Grants [BB/P012523/1, BB/P012574/1]; STFC/CCP4 [7920 S2 2020 007]

Published
2023
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25. The CCP4 suite: integrative software for macromolecular crystallography

Author

Royal Society (UK), Engineering and Physical Sciences Research Council (UK), European Commission, Medical Research Council (UK), Federal Ministry of Education and Research (Germany), German Research Foundation, Institute of Geology of the Czech Academy of Sciences, Netherlands Organization for Scientific Research, Dutch Cancer Society, Wellcome Trust, Ministerio de Ciencia e Innovación (España), Agencia Estatal de Investigación (España), Agirre, Jon, Atanasova, Mihaela, Bagdonas, Haroldas, Ballard, Charles B., Basle, A., Beilsten-Edmands, James, Borges, Rafael J., Brown, D. G., Burgos-Mármol, J. Javier, Berrisford, J., Bond, Paul S., Caballero, Iracema, Catapano, Lucrezia, Chojnowski, G., Cook, Atlanta G., Cowtan, K., Croll, Tristan I., Debreczeny, Judith E., Devenish, Nicholas E., Dodson, Eleanor J., Drevon, Tarik R., Emsley, Paul, Evans, Gwyndaf, Evans, Phil R., Fando, M., Foadi, James, Fuentes-Montero, Luis, Garman, Elspeth F., Gerstel, Markus, Gildea, Richard J., Hatti, Kaushik, Hekkelman, Maarten L., Heuser, Philipp, Wen Hoh, Soon, Hough, Michael A., Jenkins, Huw T., Jiménez, Elisabet, Joosten, Robbie P., Keegan, R. M., Keep, Nicholas, Krissinel, E., Kolenko, Petr, Kovalevskiy, O., Lamzin, V., Lawson, David M., Lebedev, Andrey, Leslie, A. G. W., Lohkamp, B., Long, Fei, Maly, Martin, McCoy, Airlie J., McNicholas, S., Medina, Ana, Millán, Claudia, Murray, James W., Murshudov, Garib, Nicholls, R. A., Noble, Martin E. M., Oeffner, Robert D., Pannu, Navraj S., Parkhurst, James M., Pearce, Nicholas, Pereira, Joana, Perrakis, Anastassis, Powell, Harold R., Read, Randy J., Rigden, D. J., Rochira, William, Sammito, Massimo, Sánchez Rodríguez, Filomeno, Sheldrick, George M., Shelley, Kathryn L., Simkovic, Felix, Simpkin, A. J., Skubák, P., Sobolev, Egor, Steiner, Roberto A., Stevenson, Kyle, Tews, I., Thomas, J. M. H., Thorn, Andrea, Triviño, Josep, Uski, V., Usón, Isabel, Vagin, Alexei, Velankar, Sameer, Vollmar, Melanie, Walden, Helen, Waterman, David, Wilson, Keith S., Winn, Martyn D., Winter, Graeme, Wojdyr, M., Yamashita, Keitaro, Royal Society (UK), Engineering and Physical Sciences Research Council (UK), European Commission, Medical Research Council (UK), Federal Ministry of Education and Research (Germany), German Research Foundation, Institute of Geology of the Czech Academy of Sciences, Netherlands Organization for Scientific Research, Dutch Cancer Society, Wellcome Trust, Ministerio de Ciencia e Innovación (España), Agencia Estatal de Investigación (España), Agirre, Jon, Atanasova, Mihaela, Bagdonas, Haroldas, Ballard, Charles B., Basle, A., Beilsten-Edmands, James, Borges, Rafael J., Brown, D. G., Burgos-Mármol, J. Javier, Berrisford, J., Bond, Paul S., Caballero, Iracema, Catapano, Lucrezia, Chojnowski, G., Cook, Atlanta G., Cowtan, K., Croll, Tristan I., Debreczeny, Judith E., Devenish, Nicholas E., Dodson, Eleanor J., Drevon, Tarik R., Emsley, Paul, Evans, Gwyndaf, Evans, Phil R., Fando, M., Foadi, James, Fuentes-Montero, Luis, Garman, Elspeth F., Gerstel, Markus, Gildea, Richard J., Hatti, Kaushik, Hekkelman, Maarten L., Heuser, Philipp, Wen Hoh, Soon, Hough, Michael A., Jenkins, Huw T., Jiménez, Elisabet, Joosten, Robbie P., Keegan, R. M., Keep, Nicholas, Krissinel, E., Kolenko, Petr, Kovalevskiy, O., Lamzin, V., Lawson, David M., Lebedev, Andrey, Leslie, A. G. W., Lohkamp, B., Long, Fei, Maly, Martin, McCoy, Airlie J., McNicholas, S., Medina, Ana, Millán, Claudia, Murray, James W., Murshudov, Garib, Nicholls, R. A., Noble, Martin E. M., Oeffner, Robert D., Pannu, Navraj S., Parkhurst, James M., Pearce, Nicholas, Pereira, Joana, Perrakis, Anastassis, Powell, Harold R., Read, Randy J., Rigden, D. J., Rochira, William, Sammito, Massimo, Sánchez Rodríguez, Filomeno, Sheldrick, George M., Shelley, Kathryn L., Simkovic, Felix, Simpkin, A. J., Skubák, P., Sobolev, Egor, Steiner, Roberto A., Stevenson, Kyle, Tews, I., Thomas, J. M. H., Thorn, Andrea, Triviño, Josep, Uski, V., Usón, Isabel, Vagin, Alexei, Velankar, Sameer, Vollmar, Melanie, Walden, Helen, Waterman, David, Wilson, Keith S., Winn, Martyn D., Winter, Graeme, Wojdyr, M., and Yamashita, Keitaro

Abstract

The Collaborative Computational Project No. 4 (CCP4) is a UK-led international collective with a mission to develop, test, distribute and promote software for macromolecular crystallography. The CCP4 suite is a multiplatform collection of programs brought together by familiar execution routines, a set of common libraries and graphical interfaces. The CCP4 suite has experienced several considerable changes since its last reference article, involving new infrastructure, original programs and graphical interfaces. This article, which is intended as a general literature citation for the use of the CCP4 software suite in structure determination, will guide the reader through such transformations, offering a general overview of the new features and outlining future developments. As such, it aims to highlight the individual programs that comprise the suite and to provide the latest references to them for perusal by crystallographers around the world.

Published
2023

36. High-resolution mapping of metal ions reveals principles of surface layer assembly in Caulobacter crescentus cells

Author

Herdman, Matthew, primary, von Kügelgen, Andriko, additional, Kureisaite-Ciziene, Danguole, additional, Duman, Ramona, additional, El Omari, Kamel, additional, Garman, Elspeth F., additional, Kjaer, Andreas, additional, Kolokouris, Dimitrios, additional, Löwe, Jan, additional, Wagner, Armin, additional, Stansfeld, Phillip J., additional, and Bharat, Tanmay A.M., additional

Published
2022
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41. Variability in X-ray induced effects in [Rh(COD)Cl]2 with changing experimental parameters.

Author

Fernando, Nathalie K., Boström, Hanna L. B., Murray, Claire A., Owen, Robin L., Thompson, Amber L., Dickerson, Joshua L., Garman, Elspeth F., Cairns, Andrew B., and Regoutz, Anna

Abstract

X-ray characterisation methods have undoubtedly enabled cutting-edge advances in all aspects of materials research. Despite the enormous breadth of information that can be extracted from these techniques, the challenge of radiation-induced sample change and damage remains prevalent. This is largely due to the emergence of modern, high-intensity X-ray source technologies and the growing potential to carry out more complex, longer duration in situ or in operando studies. The tunability of synchrotron beamlines enables the routine application of photon energy-dependent experiments. This work explores the structural stability of [Rh(COD)Cl]2, a widely used catalyst and precursor in the chemical industry, across a range of beamline parameters that target X-ray energies of 8 keV, 15 keV, 18 keV and 25 keV, on a powder X-ray diffraction synchrotron beamline at room temperature. Structural changes are discussed with respect to absorbed X-ray dose at each experimental setting associated with the respective photon energy. In addition, the X-ray radiation hardness of the catalyst is discussed, by utilising the diffraction data collected at the different energies to determine a dose limit, which is often considered in protein crystallography and typically overlooked in small molecule crystallography. This work not only gives fundamental insight into how damage manifests in this organometallic catalyst, but will encourage careful consideration of experimental X-ray parameters before conducting diffraction on similar radiation-sensitive organometallic materials. [ABSTRACT FROM AUTHOR]

Published
2022
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44. AlphaFold and the future of structural biology.

Author

Read, Randy J., Baker, Edward N., Bond, Charles S., Garman, Elspeth F., and van Raaij, Mark J.

Subjects
PROTEIN structure prediction, BIOLOGY
Abstract

This editorial acknowledges the transformative impact of new machine‐learning methods, such as the use of AlphaFold, but also makes the case for the continuing need for experimental structural biology. [ABSTRACT FROM AUTHOR]

Published
2023
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48. Zinc determines dynamical properties and aggregation kinetics of human insulin

Author

Pounot, Kevin, Grime, Geoffrey W., Longo, Alessandro, Zamponi, Michaela, Noferini, Daria, Cristiglio, Viviana, Seydel, Tilo, Garman, Elspeth F., Weik, Martin, Foderà, Vito, Schirò, Giorgio, Pounot, Kevin, Grime, Geoffrey W., Longo, Alessandro, Zamponi, Michaela, Noferini, Daria, Cristiglio, Viviana, Seydel, Tilo, Garman, Elspeth F., Weik, Martin, Foderà, Vito, and Schirò, Giorgio

Abstract

Protein aggregation is a widespread process leading to deleterious consequences in the organism, with amyloid aggregates being important not only in biology but also for drug design and biomaterial production. Insulin is a protein largely used in diabetes treatment, and its amyloid aggregation is at the basis of the so-called insulin-derived amyloidosis. Here, we uncover the major role of zinc in both insulin dynamics and aggregation kinetics at low pH, in which the formation of different amyloid superstructures (fibrils and spherulites) can be thermally induced. Amyloid aggregation is accompanied by zinc release and the suppression of water-sustained insulin dynamics, as shown by particle-induced x-ray emission and x-ray absorption spectroscopy and by neutron spectroscopy, respectively. Our study shows that zinc binding stabilizes the native form of insulin by facilitating hydration of this hydrophobic protein and suggests that introducing new binding sites for zinc can improve insulin stability and tune its aggregation propensity.

Published
2021

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