@article {49223,
	title = {Atomic resolution cryo-EM structure of β-galactosidase.},
	journal = {Structure (London, England : 1993)},
	volume = {26},
	year = {2018},
	month = {2018 Apr 30},
	pages = {848},
	abstract = {<p>The advent of direct electron detectors has enabled the routine use of single-particle cryo-electron microscopy (EM) approaches to determine structures of a variety of protein complexes at near-atomic resolution. Here, we report the development of methods to account for local variations in defocus and beam-induced drift, and the implementation of a data-driven dose compensation scheme that significantly improves the extraction of high-resolution information recorded during exposure of the specimen to the electron beam. These advances enable determination of a cryo-EM density map for β-galactosidase bound to the inhibitor phenylethyl β-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at \~{} 1.5\&nbsp;{\r A} resolution. Using this density map in conjunction with constrained molecular dynamics simulations provides a measure of the local flexibility of the non-covalently bound inhibitor and offers further opportunities for structure-guided inhibitor design.</p>
},
	issn = {1878-4186},
	doi = {10.1016/j.str.2018.04.004},
	author = {Bartesaghi, Alberto and Aguerrebere, Cecilia and Falconieri, Veronica and Banerjee, Soojay and Earl, Lesley A and Zhu, Xing and Grigorieff, Nikolaus and Milne, Jacqueline L S and Sapiro, Guillermo and Wu, Xiongwu and Subramaniam, Sriram}
}
