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@ARTICLE{Kierspel:593878,
author = {Kierspel, Thomas and Kadek, Alan and Barran, Perdita and
Bellina, Bruno and Bijedic, Adi and Brodmerkel, Maxim N. and
Commandeur, Jan and Caleman, Carl and Damjanovic, Tomislav
and Dawod, Ibrahim and De Santis, Emiliano and Lekkas,
Alexandros and Lorenzen, Kristina and Morillo, Luis López
and Mandl, Thomas and Marklund, Erik G. and Papanastasiou,
Dimitris and Ramakers, Lennart A. I. and Schweikhard, Lutz
and Simke, Florian and Sinelnikova, Anna and Smyrnakis,
Athanasios and Timneanu, Nicusor and Uetrecht, Charlotte},
title = {{C}oherent diffractive imaging of proteins and viral
capsids: simulating {MS} {SPIDOC}},
journal = {Analytical and bioanalytical chemistry},
volume = {415},
number = {18},
issn = {1618-2642},
address = {Heidelberg},
publisher = {Springer},
reportid = {PUBDB-2023-05544},
pages = {4209 - 4220},
year = {2023},
note = {This is an open access article. According to the licence we
have to provide the link to the licence and indicate if
changes were made.
http://creativecommons.org/licenses/by/4.0/, no changes},
abstract = {MS SPIDOC is a novel sample delivery system designed for
single (isolated) particle imaging at X-ray Free-Electron
Lasers that is adaptable towards most large-scale facility
beamlines. Biological samples can range from small proteins
to MDa particles. Following nano-electrospray ionization,
ionic samples can be m/z-filtered and structurally separated
before being oriented at the interaction zone. Here, we
present the simulation package developed alongside this
prototype. The first part describes how the front-to-end ion
trajectory simulations have been conducted. Highlighted is a
quadrant lens; a simple but efficient device that steers the
ion beam within the vicinity of the strong DC orientation
field in the interaction zone to ensure spatial overlap with
the X-rays. The second part focuses on protein orientation
and discusses its potential with respect to diffractive
imaging methods. Last, coherent diffractive imaging of
prototypical T = 1 and T = 3 norovirus capsids is shown. We
use realistic experimental parameters from the SPB/SFX
instrument at the European XFEL to demonstrate that low-
resolution diffractive imaging data (q < 0.3 nm$^{−1}$)
can be collected with only a few X-ray pulses. Such
low-resolution data are sufficient to distinguish between
both symmetries of the capsids, allowing to probe low
abundant species in a beam if MS SPIDOC is used as sample
delivery.},
cin = {CSSB-LIV/DESY-CU / CFEL-I},
cid = {$I:(DE-H253)CSSB-LIV_DESY-CU-20220525$ /
I:(DE-H253)CFEL-I-20161114},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633) / MS SPIDOC - Mass Spectrometry for
Single Particle Imaging of Dipole Oriented protein Complexes
(801406) / 05K22PSA - Verbundprojekt 05K2022 - 2021-05988
SAXFELS: Kleinwinkel-Röntgen-Freie-Elektronenlaser-Streuung
(BMBF-05K22PSA)},
pid = {G:(DE-HGF)POF4-633 / G:(EU-Grant)801406 /
G:(DE-Ds200)BMBF-05K22PSA},
experiment = {EXP:(DE-MLZ)NOSPEC-20140101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:37014373},
UT = {WOS:000963181300001},
doi = {10.1007/s00216-023-04658-y},
url = {https://bib-pubdb1.desy.de/record/593878},
}