Document Type
Article
Publication Date
2018
DOI
10.3390/molecules23030610
Publication Title
Molecules
Volume
23
Issue
3
Pages
610 (14 pages)
Abstract
Cryo-electron microscopy (cryo-EM) is a structure determination method for large molecular complexes. As more and more atomic structures are determined using this technique, it is becoming possible to perform statistical characterization of side-chain conformations. Two data sets were involved to characterize block lengths for each of the 18 types of amino acids. One set contains 9131 structures resolved using X-ray crystallography from density maps with better than or equal to 1.5 Å resolutions, and the other contains 237 protein structures derived from cryo-EM density maps with 2-4 Å resolutions. The results show that the normalized probability density function of block lengths is similar between the X-ray data set and the cryo-EM data set for most of the residue types, but differences were observed for ARG, GLU, ILE, LYS, PHE, TRP, and TYR for which conformations with certain shorter block lengths are more likely to be observed in the cryo-EM set with 2-4 Å resolutions.
Original Publication Citation
Chen, L., He, J., Sazzed, S., & Walker, R. (2018). An investigation of atomic structures derived from x-ray crystallography and cryo-electron microscopy using distal blocks of side-chains. Molecules, 23(3), 610. doi:http://dx.doi.org/10.3390/molecules23030610
Repository Citation
Chen, L., He, J., Sazzed, S., & Walker, R. (2018). An investigation of atomic structures derived from x-ray crystallography and cryo-electron microscopy using distal blocks of side-chains. Molecules, 23(3), 610. doi:http://dx.doi.org/10.3390/molecules23030610
Comments
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license .(http://creativecommons.org/licenses/by/4.0/).