Zobrazeno 1 - 10
of 291
pro vyhledávání: '"Rick P, Millane"'
Publikováno v:
IUCrJ, Vol 9, Iss 5, Pp 648-665 (2022)
A procedure is described for direct phase determination in protein crystallography, applicable to crystals with high solvent content. The procedure requires only the diffraction data and an estimate of the solvent content as input. Direct phase deter
Externí odkaz:
https://doaj.org/article/fd9e14cb2da449db85ba08772c42e32a
Autor:
Carolin Seuring, Kartik Ayyer, Eleftheria Filippaki, Miriam Barthelmess, Jean-Nicolas Longchamp, Philippe Ringler, Tommaso Pardini, David H. Wojtas, Matthew A. Coleman, Katerina Dörner, Silje Fuglerud, Greger Hammarin, Birgit Habenstein, Annette E. Langkilde, Antoine Loquet, Alke Meents, Roland Riek, Henning Stahlberg, Sébastien Boutet, Mark S. Hunter, Jason Koglin, Mengning Liang, Helen M. Ginn, Rick P. Millane, Matthias Frank, Anton Barty, Henry N. Chapman
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
The structures of amyloid fibres are currently primarily studied through solid state NMR and cryo-EM. Here the authors present a free-standing graphene support device that allows diffraction imaging of non-crystalline amyloid fibrils with single X-ra
Externí odkaz:
https://doaj.org/article/0f29de3d658a4701815f6d96e5366ab4
Autor:
David H. Wojtas, Kartik Ayyer, Mengning Liang, Estelle Mossou, Filippo Romoli, Carolin Seuring, Kenneth R. Beyerlein, Richard J. Bean, Andrew J. Morgan, Dominik Oberthuer, Holger Fleckenstein, Michael Heymann, Cornelius Gati, Oleksandr Yefanov, Miriam Barthelmess, Eirini Ornithopoulou, Lorenzo Galli, P. Lourdu Xavier, Wai Li Ling, Matthias Frank, Chun Hong Yoon, Thomas A. White, Saša Bajt, Anna Mitraki, Sebastien Boutet, Andrew Aquila, Anton Barty, V. Trevor Forsyth, Henry N. Chapman, Rick P. Millane
Publikováno v:
IUCrJ, Vol 4, Iss 6, Pp 795-811 (2017)
Serial diffraction data collected at the Linac Coherent Light Source from crystalline amyloid fibrils delivered in a liquid jet show that the fibrils are well oriented in the jet. At low fibril concentrations, diffraction patterns are recorded from s
Externí odkaz:
https://doaj.org/article/8f9885fc0d6b468c9e75f6f80878cb8b
Autor:
Rick P. Millane, Pradeep K. Luther
Publikováno v:
Journal of Muscle Research and Cell Motility.
Early x-ray diffraction studies of muscle revealed spacings larger than the basic thick filament lattice spacing and led to a number of speculations on the mutual rotations of the filaments in the myosin lattice. The nature of the arrangements of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbfa11aa76177feae2f0fb4daa70467f
https://doi.org/10.1007/s10974-023-09642-8
https://doi.org/10.1007/s10974-023-09642-8
Autor:
Romain D, Arnal, Rick P, Millane
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 78:249-261
Filamentary and rod-like assemblies are ubiquitous in biological systems, and single such assemblies can form one-dimensional (1D) crystals. New, intense X-ray sources, such as X-ray free-electron lasers, make it feasible to measure diffraction data
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4905822651e3f2abde9c905f52c73b8
https://doi.org/10.1107/s2053273322001942
https://doi.org/10.1107/s2053273322001942
Autor:
Rick P. Millane, David H. Wojtas, Chun Hong Yoon, Nicholas D. Blakeley, Philip J. Bones, Abhishek Goyal, John M. Squire, Pradeep K. Luther
Publikováno v:
J R Soc Interface
Geometric frustration results from an incompatibility between minimum energy arrangements and the geometry of a system, and gives rise to interesting and novel phenomena. Here, we report geometric frustration in a native biological macromolecular sys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b644fd020a02c6ba381c6edb9499d483
https://europepmc.org/articles/PMC8672065/
https://europepmc.org/articles/PMC8672065/
Publikováno v:
IUCrJ. 9(Pt 5)
A procedure is described for direct phase determination in protein crystallography, applicable to crystals with high solvent content. The procedure requires only the diffraction data and an estimate of the solvent content as input. Direct phase deter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8eb5f75e7663658de687241907ab5990
https://pubmed.ncbi.nlm.nih.gov/36071801
https://pubmed.ncbi.nlm.nih.gov/36071801
Publikováno v:
IVCNZ
X-ray free-electron lasers (XFELs) are opening new frontiers in structural biology. The extreme brilliance of these highly coherent X-ray sources allows for ever smaller crystals to be used while still being able to diffract enough photons to provide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12ee67be28bed36e82b95a704a102983
https://doi.org/10.1109/ivcnz51579.2020.9290623
https://doi.org/10.1109/ivcnz51579.2020.9290623
Autor:
Rick P. Millane, Juraj Knoska, Sébastien Boutet, Oleksandr Yefanov, Ruojie Sha, Carolin Seuring, Kartik Ayyer, David A. Bushnell, Mengning Liang, Anton Barty, Roger D. Kornberg, P. Lourdu Xavier, Nadrian C. Seeman, Henry N. Chapman, Saša Bajt
Publikováno v:
Biophysical journal 118(3), 137a-138a (2020). doi:10.1016/j.bpj.2019.11.877
64th Annual Biophysical Society Meeting, San Diego, 2020-02-15-2020-02-19
64th Annual Biophysical Society Meeting, San Diego, 2020-02-15-2020-02-19
64th Annual Biophysical Society Meeting, San Diego, 15 Feb 2020 - 19 Feb 2020; Biophysical journal 118(3), 137a - 138a (2020). doi:10.1016/j.bpj.2019.11.877
Outrunning radiation damage, highly intense femtosecond pulses of X-ray free-electron la
Outrunning radiation damage, highly intense femtosecond pulses of X-ray free-electron la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21005968d3100f24fb13029cdf5563a1
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 74:537-544
Phasing of diffraction data from two-dimensional crystals using only minimal molecular envelope information is investigated by simulation. Two-dimensional crystals are an attractive target for studying membrane proteins using X-ray free-electron lase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c549307fc6be1521328050060f2264c
https://doi.org/10.1107/s2053273318008707
https://doi.org/10.1107/s2053273318008707