5A1A

2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor

Summary for 5A1A

• Entry DOI: 10.2210/pdb5a1a/pdb
• EMDB information: 2984
• Descriptor: BETA-GALACTOSIDASE, 2-phenylethyl 1-thio-beta-D-galactopyranoside, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase, near-atomic, near-atomic resolution cryo-electron microscopy, single- particle cryo-em, protein complexes, petg
• Biological source: ESCHERICHIA COLI K-12
• Total number of polymer chains: 4
• Total formula weight: 467060.60

Authors

Bartesaghi, A.,Merk, A.,Banerjee, S.,Matthies, D.,Wu, X.,Milne, J.,Subramaniam, S. (deposition date: 2015-04-29, release date: 2015-05-06, Last modification date: 2024-05-08)

Primary citation

Bartesaghi, A.,Merk, A.,Banerjee, S.,Matthies, D.,Wu, X.,Milne, J.,Subramaniam, S.
2.2 A Resolution Cryo-Em Structure of Beta-Galactosidase in Complex with a Cell-Permeant Inhibitor
Science, 348:1147-, 2015

PubMed Abstract: Cryo-electron microscopy (cryo-EM) is rapidly emerging as a powerful tool for protein structure determination at high resolution. Here we report the structure of a complex between Escherichia coli β-galactosidase and the cell-permeant inhibitor phenylethyl β-D-thiogalactopyranoside (PETG), determined by cryo-EM at an average resolution of ~2.2 angstroms (Å). Besides the PETG ligand, we identified densities in the map for ~800 water molecules and for magnesium and sodium ions. Although it is likely that continued advances in detector technology may further enhance resolution, our findings demonstrate that preparation of specimens of adequate quality and intrinsic protein flexibility, rather than imaging or image-processing technologies, now represent the major bottlenecks to routinely achieving resolutions close to 2 Å using single-particle cryo-EM.

PubMed: 25953817
DOI: 10.1126/SCIENCE.AAB1576

Experimental method

ELECTRON MICROSCOPY (2.2 Å)