Search

Your search keyword '"Martin-Garcia, Jose Manuel"' showing total 15 results
Start Over Author "Martin-Garcia, Jose Manuel"
15 results on '"Martin-Garcia, Jose Manuel"'

1. New insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis

Author

Moreno, Andrea, Quereda-Moraleda, Isabel, Lozano-Vallhonrat, Celia, Buñuel-Escudero, María, Botha, Sabine, Kupitz, Christopher, Lisova, Stella, Sierra, Ray, Mariani, Valerio, Schleissner, Pamela, Gee, Leland B., Dörner, Katerina, Schmidt, Christina, Han, Huijong, Kloos, Marco, Smyth, Peter, Valerio, Joana, Schulz, Joachim, de Wijn, Raphael, Melo, Diogo V.M., Round, Adam, Trost, Fabian, Sobolev, Egor, Juncheng, E., Sikorski, Marcin, Bean, Richard, Martínez-Júlvez, Marta, Martin-Garcia, Jose Manuel, and Medina, Milagros

Published
2024
Full Text
View/download PDF

2. Heterogeneity in M. tuberculosis β-lactamase inhibition by Sulbactam

Author

Malla, Tek Narsingh, Zielinski, Kara, Aldama, Luis, Bajt, Sasa, Feliz, Denisse, Hayes, Brendon, Hunter, Mark, Kupitz, Christopher, Lisova, Stella, Knoska, Juraj, Martin-Garcia, Jose Manuel, Mariani, Valerio, Pandey, Suraj, Poudyal, Ishwor, Sierra, Raymond G., Tolstikova, Alexandra, Yefanov, Oleksandr, Yoon, Chung Hong, Ourmazd, Abbas, Fromme, Petra, Schwander, Peter, Barty, Anton, Chapman, Henry N., Stojkovic, Emina A., Batyuk, Alexander, Boutet, Sébastien, Phillips, Jr., George N., Pollack, Lois, and Schmidt, Marius

Published
2023
Full Text
View/download PDF

3. Structural dynamics and functional cooperativity of humanNQO1 by ambient temperature serial crystallography andsimulations

Author

Ministerio de Ciencia e Innovación (España), Ministerio de Ciencia, Innovación y Universidades (España), Comunidad de Madrid, Junta de Andalucía, Gobierno de Aragón, Agencia Estatal de Investigación (España), Gavira Gallardo, J. A. [0000-0002-7386-6484], Medina, Milagros [0000-0001-8743-0182], Martin-Garcia, Jose Manuel [0000-0002-4558-3858], Grieco, Alice, Boneta, Sergio, Gavira Gallardo, J. A., Pey, Ángel L., Basu, Shibom, Orlans, Julien, Sanctis, Daniele de, Medina, Milagros, Martin-Garcia, Jose Manuel, Ministerio de Ciencia e Innovación (España), Ministerio de Ciencia, Innovación y Universidades (España), Comunidad de Madrid, Junta de Andalucía, Gobierno de Aragón, Agencia Estatal de Investigación (España), Gavira Gallardo, J. A. [0000-0002-7386-6484], Medina, Milagros [0000-0001-8743-0182], Martin-Garcia, Jose Manuel [0000-0002-4558-3858], Grieco, Alice, Boneta, Sergio, Gavira Gallardo, J. A., Pey, Ángel L., Basu, Shibom, Orlans, Julien, Sanctis, Daniele de, Medina, Milagros, and Martin-Garcia, Jose Manuel

Abstract

The human NQO1 (hNQO1) is a flavin adenine nucleotide (FAD)-dependentoxidoreductase that catalyzes the two-electron reduction of quinones to hydro-quinones, being essential for the antioxidant defense system, stabilization oftumor suppressors, and activation of quinone-based chemotherapeutics. More-over, it is overexpressed in several tumors, which makes it an attractive cancerdrug target. To decipher new structural insights into the flavin reductive half-reaction of the catalytic mechanism of hNQO1, we have carried serial crystal-lography experiments at new ID29 beamline of the ESRF to determine, to thebest of our knowledge, the first structure of the hNQO1 in complex withNADH. We have also performed molecular dynamics simulations of freehNQO1 and in complex with NADH. This is the first structural evidence thatthe hNQO1 functional cooperativity is driven by structural communicationbetween the active sites through long-range propagation of cooperative effectsacross the hNQO1 structure. Both structural results and MD simulations havesupported that the binding of NADH significantly decreases protein dynamics

Published
2024

4. Cyclic Olefin Copolymer-Based Fixed-Target Sample Delivery Device for Protein X-ray Crystallography

Author

Manna, Abhik, Sonker, Mukul, Koh, Domin, Steiger, Michael, Ansari, Adil, Hu, Hao, Quereda-Moraleda, Isabel, Grieco, Alice, Doppler, Diandra, de Sanctis, Daniele, Basu, Shibom, Orlans, Julien, Rose, Samuel L., Botha, Sabine, Martin-Garcia, Jose Manuel, and Ros, Alexandra

Abstract

Serial macromolecular X-ray crystallography plays an important role in elucidating protein structures and consequently progressing the field of targeted therapeutics. The use of pulsed beams at different repetition frequencies requires the development of various sample-conserving injection strategies to minimize sample wastage between X-ray exposures. Fixed-target sample delivery methods that use solid support to hold the crystals in the X-ray beam path are gaining interest as a sample-conserving delivery system for X-ray crystallography with high crystal hit rates. Here, we present a novel fixed-target microfluidic system for delivering protein microcrystals to X-ray beams for diffraction data collection and structure determination. The fixed-target design consists of 3 symmetric sections arranged in an area of 1 in. × 1 in. with up to 18,000 crystal traps per device. Each trap is targeted to hold one crystal up to 50 μm in size in the largest dimension. The device has been fabricated using cyclic olefin copolymer (COC) for high-quality diffraction data collection with low background scattering induced through the fixed-target material. The newly developed fixed-target device is designed for vacuum compatibility which will enable the use in vacuum experimental chambers of X-ray radiation sources including the newly developed, first-of-its-kind compact X-ray light source (CXLS), which is currently in commissioning at Arizona State University. To assess the validity of the COC device, serial crystallography experiments were performed on the model protein lysozyme at the new European Synchrotron Radiation Facility-Extremely Brilliant Source (ESRF-EBS) beamline ID29. A 1.6 Å crystal structure of the protein was solved, demonstrating that, in general, the COC device can be used to generate high-quality data from macromolecular crystals at the CXLS and synchrotron radiation sources, which holds enormous potential for advancing the field of protein structure determination by fixed-target X-ray crystallography.

Published
2024
Full Text
View/download PDF

5. Innovative Strategies in X-ray Crystallography for Exploring Structural Dynamics and Reaction Mechanisms in Metabolic Disorders.

Author

Grieco, Alice, Quereda-Moraleda, Isabel, and Martin-Garcia, Jose Manuel

Subjects
X-ray crystallography, G protein coupled receptors, CRYSTALLOIDS (Botany), X-ray lasers, METABOLIC disorders
Abstract

Enzymes are crucial in metabolic processes, and their dysfunction can lead to severe metabolic disorders. Structural biology, particularly X-ray crystallography, has advanced our understanding of these diseases by providing 3D structures of pathological enzymes. However, traditional X-ray crystallography faces limitations, such as difficulties in obtaining suitable protein crystals and studying protein dynamics. X-ray free-electron lasers (XFELs) have revolutionized this field with their bright and brief X-ray pulses, providing high-resolution structures of radiation-sensitive and hard-to-crystallize proteins. XFELs also enable the study of protein dynamics through room temperature structures and time-resolved serial femtosecond crystallography, offering comprehensive insights into the molecular mechanisms of metabolic diseases. Understanding these dynamics is vital for developing effective therapies. This review highlights the contributions of protein dynamics studies using XFELs and synchrotrons to metabolic disorder research and their application in designing better therapies. It also discusses G protein-coupled receptors (GPCRs), which, though not enzymes, play key roles in regulating physiological systems and are implicated in many metabolic disorders. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

6. Minimized Sample Consumption for Time-Resolved Serial Crystallography Applied to the Redox Cycle of Human NQO1

Author

Doppler, Diandra, primary, Grieco, Alice, additional, Koh, Domin, additional, Manna, Abhik, additional, Ansari, Adil, additional, Alvarez, Roberto, additional, Karpos, Konstantinos, additional, Le, Hung, additional, Sonker, Mukul, additional, Ketawala, Gihan, additional, Mahmud, Samira, additional, Quereda Moraleda, Isabel, additional, Pey, Angel Luis, additional, Letrun, Roman, additional, Doerner, Katerina, additional, Koliyadu, Jayanath C. P., additional, de Wijn, Raphael, additional, Bielecki, Johan, additional, Han, Huijong, additional, Kim, Chan, additional, Koua, Faisal, additional, Round, Adam, additional, Sarma, Abhisakh, additional, Sato, Tokushi, additional, Schmidt, Christina, additional, Vakili, Mohammad, additional, Zabelskii, Dmitrii, additional, Bean, Richard, additional, Mancuso, Adrian P., additional, Schulz, Joachim, additional, Fromme, Raimund, additional, Medina, Milagros, additional, Grant, Thomas D, additional, Fromme, Petra, additional, Kirian, Richard A., additional, Botha, Sabine, additional, Martin Garcia, Jose Manuel, additional, and Ros, Alexandra, additional

Published
2024
Full Text
View/download PDF

9. Modular droplet injector for sample conservation providing new structural insight for the conformational heterogeneity in the disease-associated NQO1 enzyme

Author

Doppler, Diandra, primary, Sonker, Mukul, additional, Egatz-Gomez, Ana, additional, Grieco, Alice, additional, Zaare, Sahba, additional, Jernigan, Rebecca, additional, Meza-Aguilar, Jose Domingo, additional, Rabbani, Mohammad T., additional, Manna, Abhik, additional, Alvarez, Roberto C., additional, Karpos, Konstantinos, additional, Cruz Villarreal, Jorvani, additional, Nelson, Garrett, additional, Yang, Jay-How, additional, Carrion, Jackson, additional, Morin, Katherine, additional, Ketawala, Gihan K., additional, Pey, Angel L., additional, Ruiz-Fresneda, Miguel Angel, additional, Pacheco-Garcia, Juan Luis, additional, Hermoso, Juan A., additional, Nazari, Reza, additional, Sierra, Raymond, additional, Hunter, Mark S., additional, Batyuk, Alexander, additional, Kupitz, Christopher J., additional, Sublett, Robert E., additional, Lisova, Stella, additional, Mariani, Valerio, additional, Boutet, Sébastien, additional, Fromme, Raimund, additional, Grant, Thomas D., additional, Botha, Sabine, additional, Fromme, Petra, additional, Kirian, Richard A., additional, Martin-Garcia, Jose Manuel, additional, and Ros, Alexandra, additional

Published
2023
Full Text
View/download PDF

10. Segmented flow generator for serial crystallography at the European X-ray free electron laser

Author

Echelmeier, Austin, Cruz Villarreal, Jorvani, Messerschmidt, Marc, Kim, Daihyun, Coe, Jesse, Thifault, Darren, Botha, Sabine, Egatz-Gomez, Ana, Gandhi, Sahir, Brehm, Gerrit, Conrad, Chelsie E., Hansen, Debra T., Madsen, Caleb, Bajt, Saša, Meza-Aguilar, J. Domingo, Oberthür, Dominik, Wiedorn, Max Oliver, Fleckenstein, Holger, Mendez, Derek, Knoška, Juraj, Martin-Garcia, Jose Manuel, Hu, Hao, Lisova, Stella, Allahgholi, Aschkan, Gevorkov, Yaroslav, Ayyer, Kartik, Aplin, Steven, Ginn, Helen Mary, Graafsma, Heinz, Morgan, Andrew J., Greiffenberg, Dominic, Klujev, Alexander, Laurus, Torsten, Pöhlsen, Jennifer, Trunk, Ulrich, Mezza, Davide, Schmidt, Bernd, Kuhn, Manuela, Fromme, Raimund, Sztuk-Dambietz, Jolanta, Raab, Natascha, Hauf, Steffen, Silenzi, Alessandro, Michelat, Thomas, Xu, Chen, Danilevski, Cyril, Parenti, Andrea, Mekinda, Leonce, Weinhausen, Britta, Mills, Grant, Vagovic, Patrik, Kim, Yoonhee, Kirkwood, Henry, Bean, Richard, Bielecki, Johan, Stern, Stephan, Giewekemeyer, Klaus, Round, Adam R., Schulz, Joachim, Dörner, Katerina Henrike, Grant, Thomas D., Mariani, Valerio, Barty, Anton, Mancuso, Adrian P., Weierstall, Uwe, Spence, John C. H., Chapman, Henry N., Zatsepin, Nadia, Fromme, Petra, Kirian, Richard A., Ros, Alexandra, Echelmeier, Austin, Cruz Villarreal, Jorvani, Messerschmidt, Marc, Kim, Daihyun, Coe, Jesse, Thifault, Darren, Botha, Sabine, Egatz-Gomez, Ana, Gandhi, Sahir, Brehm, Gerrit, Conrad, Chelsie E., Hansen, Debra T., Madsen, Caleb, Bajt, Saša, Meza-Aguilar, J. Domingo, Oberthür, Dominik, Wiedorn, Max Oliver, Fleckenstein, Holger, Mendez, Derek, Knoška, Juraj, Martin-Garcia, Jose Manuel, Hu, Hao, Lisova, Stella, Allahgholi, Aschkan, Gevorkov, Yaroslav, Ayyer, Kartik, Aplin, Steven, Ginn, Helen Mary, Graafsma, Heinz, Morgan, Andrew J., Greiffenberg, Dominic, Klujev, Alexander, Laurus, Torsten, Pöhlsen, Jennifer, Trunk, Ulrich, Mezza, Davide, Schmidt, Bernd, Kuhn, Manuela, Fromme, Raimund, Sztuk-Dambietz, Jolanta, Raab, Natascha, Hauf, Steffen, Silenzi, Alessandro, Michelat, Thomas, Xu, Chen, Danilevski, Cyril, Parenti, Andrea, Mekinda, Leonce, Weinhausen, Britta, Mills, Grant, Vagovic, Patrik, Kim, Yoonhee, Kirkwood, Henry, Bean, Richard, Bielecki, Johan, Stern, Stephan, Giewekemeyer, Klaus, Round, Adam R., Schulz, Joachim, Dörner, Katerina Henrike, Grant, Thomas D., Mariani, Valerio, Barty, Anton, Mancuso, Adrian P., Weierstall, Uwe, Spence, John C. H., Chapman, Henry N., Zatsepin, Nadia, Fromme, Petra, Kirian, Richard A., and Ros, Alexandra

Abstract

Serial femtosecond crystallography (SFX) with X-ray free electron lasers (XFELs) allows structure determination of membrane proteins and time-resolved crystallography. Common liquid sample delivery continuously jets the protein crystal suspension into the path of the XFEL, wasting a vast amount of sample due to the pulsed nature of all current XFEL sources. The European XFEL (EuXFEL) delivers femtosecond (fs) X-ray pulses in trains spaced 100 ms apart whereas pulses within trains are currently separated by 889 ns. Therefore, continuous sample delivery via fast jets wastes >99% of sample. Here, we introduce a microfluidic device delivering crystal laden droplets segmented with an immiscible oil reducing sample waste and demonstrate droplet injection at the EuXFEL compatible with high pressure liquid delivery of an SFX experiment. While achieving ~60% reduction in sample waste, we determine the structure of the enzyme 3-deoxy-D-manno-octulosonate-8-phosphate synthase from microcrystals delivered in droplets revealing distinct structural features not previously reported.

Published
2020

11. Membrane protein megahertz crystallography at the European XFEL

Author

Gisriel, Christopher, Coe, Jesse, Letrun, Romain, Yefanov, Oleksandr, Luna-Chavez, Cesar, Stander, Natasha E., Lisova, Stella, Mariani, Valerio, Kuhn, Manuela, Aplin, Steven, Grant, Thomas D., Dörner, Katerina Henrike, Sato, Tokushi, Echelmeier, Austin, Cruz Villarreal, Jorvani, Hunter, Mark S., Wiedorn, Max Oliver, Knoška, Juraj, Mazalova, Victoria, Roy-Chowdhury, Shatabdi, Yang, Jay How, Jones, Alex, Bean, Richard, Bielecki, Johan, Kim, Yoonhee, Mills, Grant, Weinhausen, Britta, Meza, Jose D., Al-Qudami, Nasser, Bajt, Saša, Brehm, Gerrit, Botha, Sabine, Boukhelef, Djelloul, Brockhauser, Sandor, Bruce, Barry D., Coleman, Matthew A., Danilevski, Cyril, Discianno, Erin, Dobson, Zachary, Fangohr, Hans, Martin-Garcia, Jose Manuel, Gevorkov, Yaroslav, Hauf, Steffen, Hosseinizadeh, Ahmad, Januschek, F., Ketawala, Gihan K., Kupitz, Christopher, Maia, Luis, Manetti, Maurizio, Messerschmidt, Marc, Michelat, Thomas, Mondal, Jyotirmoy, Ourmazd, Abbas, Previtali, Gianpietro, Sarrou, Iosifina, Schön, Silvan, Schwander, Peter, Shelby, Megan L., Silenzi, Alessandro, Sztuk-Dambietz, Jolanta, Szuba, Janusz, Turcato, Monica, White, Thomas A., Wrona, Krzysztof, Xu, Chen, Abdellatif, Mohamed H., Zook, James D., Spence, John C. H., Chapman, Henry N., Barty, Anton, Kirian, Richard A., Frank, Matthias, Ros, Alexandra, Schmidt, Marius, Fromme, Raimund, Mancuso, Adrian P., Fromme, Petra, Zatsepin, Nadia, Gisriel, Christopher, Coe, Jesse, Letrun, Romain, Yefanov, Oleksandr, Luna-Chavez, Cesar, Stander, Natasha E., Lisova, Stella, Mariani, Valerio, Kuhn, Manuela, Aplin, Steven, Grant, Thomas D., Dörner, Katerina Henrike, Sato, Tokushi, Echelmeier, Austin, Cruz Villarreal, Jorvani, Hunter, Mark S., Wiedorn, Max Oliver, Knoška, Juraj, Mazalova, Victoria, Roy-Chowdhury, Shatabdi, Yang, Jay How, Jones, Alex, Bean, Richard, Bielecki, Johan, Kim, Yoonhee, Mills, Grant, Weinhausen, Britta, Meza, Jose D., Al-Qudami, Nasser, Bajt, Saša, Brehm, Gerrit, Botha, Sabine, Boukhelef, Djelloul, Brockhauser, Sandor, Bruce, Barry D., Coleman, Matthew A., Danilevski, Cyril, Discianno, Erin, Dobson, Zachary, Fangohr, Hans, Martin-Garcia, Jose Manuel, Gevorkov, Yaroslav, Hauf, Steffen, Hosseinizadeh, Ahmad, Januschek, F., Ketawala, Gihan K., Kupitz, Christopher, Maia, Luis, Manetti, Maurizio, Messerschmidt, Marc, Michelat, Thomas, Mondal, Jyotirmoy, Ourmazd, Abbas, Previtali, Gianpietro, Sarrou, Iosifina, Schön, Silvan, Schwander, Peter, Shelby, Megan L., Silenzi, Alessandro, Sztuk-Dambietz, Jolanta, Szuba, Janusz, Turcato, Monica, White, Thomas A., Wrona, Krzysztof, Xu, Chen, Abdellatif, Mohamed H., Zook, James D., Spence, John C. H., Chapman, Henry N., Barty, Anton, Kirian, Richard A., Frank, Matthias, Ros, Alexandra, Schmidt, Marius, Fromme, Raimund, Mancuso, Adrian P., Fromme, Petra, and Zatsepin, Nadia

Abstract

The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.

Published
2019

Catalog

Books, media, physical & digital resources
See catalog results