% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Geraets:889724,
author = {Geraets, James and Pothula, Karunakar R and Schröder,
Gunnar F},
title = {{I}ntegrating cryo-{EM} and {NMR} data},
journal = {Current opinion in structural biology},
volume = {61},
issn = {0959-440X},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {FZJ-2021-00345},
pages = {173 - 181},
year = {2020},
abstract = {Single-particle cryo-electron microscopy (cryo-EM) is
increasingly used as a technique to determine the atomic
structure of challenging biological systems. Recent advances
in microscope engineering, electron detection, and image
processing have allowed the structural determination of
bigger and more flexible targets than possible with the
complementary techniques X-ray crystallography and NMR
spectroscopy. However, there exist many biological targets
for which atomic resolution cannot be currently achieved
with cryo-EM, making unambiguous determination of the
protein structure impossible. Although determining the
structure of large biological systems using solely NMR is
often difficult, highly complementary experimental
atomic-level data for each molecule can be derived from the
spectra, and used in combination with cryo-EM data. We
review here strategies with which both techniques can be
synergistically combined, in order to reach detail and
understanding unattainable by each technique acting alone;
and the types of biological systems for which such an
approach would be desirable.},
cin = {IBI-7},
ddc = {570},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
pubmed = {32028106},
UT = {WOS:000525828700024},
doi = {10.1016/j.sbi.2020.01.008},
url = {https://juser.fz-juelich.de/record/889724},
}