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-Structure paper
タイトル | 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. |
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ジャーナル・号・ページ | Science, Vol. 348, Issue 6239, Page 1147-1151, Year 2015 |
掲載日 | 2015年6月5日 |
![]() | Alberto Bartesaghi / Alan Merk / Soojay Banerjee / Doreen Matthies / Xiongwu Wu / Jacqueline L S Milne / Sriram Subramaniam / ![]() |
PubMed 要旨 | 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- ...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. |
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手法 | EM (単粒子) |
解像度 | 2.2 Å |
構造データ | |
化合物 | ![]() ChemComp-PTQ: ![]() ChemComp-MG: ![]() ChemComp-NA: ![]() ChemComp-HOH: |
由来 |
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![]() | HYDROLASE / NEAR-ATOMIC / NEAR-ATOMIC RESOLUTION CRYO-ELECTRON MICROSCOPY / SINGLE- PARTICLE CRYO-EM / PROTEIN COMPLEXES / PETG |