Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Marcel Arheit"'
Autor:
Peter Munro, Markus Oelhafen, Luis Melo Carvalho, Marcel Arheit, Marcus Brehm, Pascal Paysan, Timo Berkus, John Pavkovich, Wilko F.A.R. Verbakel, Adam Wang, Josh Star-Lack, Mingshan Sun, Dieter Seghers
Publikováno v:
Star-Lack, J, Sun, M, Oelhafen, M, Berkus, T, Pavkovich, J, Brehm, M, Arheit, M, Paysan, P, Wang, A, Munro, P, Seghers, D, Carvalho, L M & Verbakel, W F A R 2018, ' A modified McKinnon-Bates (MKB) algorithm for improved 4D cone-beam computed tomography (CBCT) of the lung ', Medical Physics, vol. 45, no. 8, pp. 3783-3799 . https://doi.org/10.1002/mp.13034
Medical Physics, 45(8), 3783-3799. AAPM-American Association of Physicists in Medicine
Medical Physics, 45(8), 3783-3799. AAPM-American Association of Physicists in Medicine
Purpose: Four-dimensional (4D) cone-beam computed tomography (CBCT) of the lung is an effective tool for motion management in radiotherapy but presents a challenge because of slow gantry rotation times. Sorting the individual projections by breathing
Publikováno v:
Journal of structural biology
In cases where ultra-flat cryo-preparations of well-ordered two-dimensional (2D) crystals are available, electron crystallography is a powerful method for the determination of the high-resolution structures of membrane and soluble proteins. However,
Publikováno v:
Structure (London England : 1993)
The secondary Na+/citrate symporter CitS of Klebsiella pneumoniae is the best-characterized member of the 2-hydroxycarboxylate transporter family. The recent projection structure gave insight into its overall structural organization. Here, we present
Autor:
Marcel Arheit, Philippe Ringler, Henning Stahlberg, Sebastian Scherer, Mohamed Chami, Julia Kowal, Venkata P. Dandey
Publikováno v:
Journal of structural biology
The introduction of direct electron detectors (DED) to cryo-electron microscopy has tremendously increased the signal-to-noise ratio (SNR) and quality of the recorded images. We discuss the optimal use of DEDs for cryo-electron crystallography, intro
Autor:
Raphaël Thierry, Marcel Arheit, Priyanka D. Abeyrathne, Daniel Castaño-Díez, Henning Stahlberg, Bryant Gipson
Publikováno v:
Methods in Molecular Biology ISBN: 9781627031752
Methods in molecular biology (Clifton N.J.)
Methods in molecular biology (Clifton N.J.)
Electron crystallography of membrane proteins uses cryo-transmission electron microscopy to record images and diffraction patterns of frozen-hydrated 2D crystals. Each two-dimensional (2D) crystal is only imaged once, at one specific tilt angle, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb5454b1c6fe1e633d1530cc435397d9
https://doi.org/10.1007/978-1-62703-176-9_11
https://doi.org/10.1007/978-1-62703-176-9_11
Autor:
Daniel Castaño-Díez, Marcel Arheit, Bryant Gipson, Xiangyan Zeng, Raphaël Thierry, Henning Stahlberg
Publikováno v:
Methods in Molecular Biology ISBN: 9781627031752
Methods in molecular biology (Clifton N.J.)
Methods in molecular biology (Clifton N.J.)
Electron crystallography of membrane proteins uses cryo-transmission electron microscopy to image frozen-hydrated 2D crystals. The processing of recorded images exploits the periodic arrangement of the structures in the images to extract the amplitud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::928dc3b8b853226f3a8e21f8d42484fc
https://doi.org/10.1007/978-1-62703-176-9_10
https://doi.org/10.1007/978-1-62703-176-9_10
Autor:
Ludovic Renault, Marcel Arheit, Henning Stahlberg, Fabian Kebbel, Mohamed Chami, Daniel Castaño-Díez, Werner Kühlbrandt, Priyanka D. Abeyrathne, Kenneth N. Goldie
Membrane protein structure determination continues to be a challenging endeavor. The key steps involved in determining the three-dimensional (3-D) structure of a membrane protein from two-dimensional (2-D) crystals are the expression and purification
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::50118301417612cd2c7aeefcf6ed7ef4
https://doi.org/10.1016/b978-0-12-374920-8.00119-3
https://doi.org/10.1016/b978-0-12-374920-8.00119-3
Autor:
Julia Kowal, Gunnar F. Schröder, Paul Baumgartner, Po-Lin Chiu, Simon Scheuring, Crina M. Nimigean, Henning Stahlberg, Marcel Arheit, Martina Rangl, Mohamed Chami
Publikováno v:
Nature communications
Nature Communications
Nature Communications, Nature Publishing Group, 2014, 5, pp.3106. ⟨10.1038/ncomms4106⟩
Nature Communications 5, (1-10) 4106 (2014). doi:10.1038/ncomms4106
Nature Communications
Nature Communications, Nature Publishing Group, 2014, 5, pp.3106. ⟨10.1038/ncomms4106⟩
Nature Communications 5, (1-10) 4106 (2014). doi:10.1038/ncomms4106
Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. H
Autor:
Henning Stahlberg, Bryant Gipson, Andreas D. Schenk, Xiangyan Zeng, Marcel Arheit, Daniel Castaño-Díez
Publikováno v:
Methods in enzymology
Electron crystallography of 2D protein crystals can determine the structure of membrane embedded proteins at high resolution. Images or electron diffraction patterns are recorded with the electron microscope of the frozen hydrated samples, and the 3D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7e5111d5fdb5570dcc7c95bbefb8594
https://infoscience.epfl.ch/record/274460
https://infoscience.epfl.ch/record/274460
Autor:
Raphaël Thierry, Bryant Gipson, Henning Stahlberg, Marcel Arheit, Daniel Castaño-Díez, Xiangyan Zeng
Publikováno v:
Methods in molecular biology (Clifton N.J.)
Methods in Molecular Biology ISBN: 9781627031752
Methods in Molecular Biology ISBN: 9781627031752
Electron crystallography of membrane proteins records images and diffraction patterns of frozen-hydrated two-dimensional (2D) crystals. To reconstruct the high-resolution three-dimensional (3D) structure of a membrane protein, a multitude of images o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b82beb1b09f79b16d43f1ff97b7f3dd1
https://infoscience.epfl.ch/record/274463
https://infoscience.epfl.ch/record/274463