TY  - JOUR
AU  - Beckers, Maximilian
AU  - Mann, Daniel
AU  - Sachse, Carsten
TI  - Structural interpretation of cryo-EM image reconstructions
JO  - Progress in biophysics & molecular biology
VL  - 160
SN  - 0079-6107
CY  - Amsterdam [u.a.]
PB  - Elsevier Science
M1  - FZJ-2020-02740
SP  - 26-36
PY  - 2021
AB  - The productivity of single-particle cryo-EM as a structure determination method has rapidly increased as many novel biological structures are being elucidated. The ultimate result of the cryo-EM experiment is an atomic model that should faithfully represent the computed image reconstruction. Although the principal approach of atomic model building and refinement from maps resembles that of the X-ray crystallographic methods, there are important differences due to the unique properties resulting from the 3D image reconstructions. In this review, we discuss the practiced work-flow from the cryo-EM image reconstruction to the atomic model. We give an overview of (i) resolution determination methods in cryo-EM including local and directional resolution variation, (ii) cryo-EM map contrast optimization including complementary map types that can help in identifying ambiguous density features, (iii) atomic model building and (iv) refinement in various resolution regimes including (v) their validation and (vi) discuss differences between X-ray and cryo-EM maps. Based on the methods originally developed for X-ray crystallography, the path from 3D image reconstruction to atomic coordinates has become an integral and important part of the cryo-EM structure determination work-flow that routinely delivers atomic models.
LB  - PUB:(DE-HGF)16
C6  - 32735944
UR  - <Go to ISI:>//WOS:000632013800005
DO  - DOI:10.1016/j.pbiomolbio.2020.07.004
UR  - https://juser.fz-juelich.de/record/878277
ER  -