ausblenden:
Schlagwörter:
CRYO-EM STRUCTURE; TRANSMISSION ELECTRON-MICROSCOPY; BEAM-INDUCED
MOTION; PHASE-PLATE; 3-DIMENSIONAL MODEL; MOLECULAR SOCIOLOGY; 26S PROTEASOME; RESOLUTION; CRYSTALLOGRAPHY; COMPLEX
Biochemistry & Molecular Biology; cryo-electron microscopy; cryo-electron tomography;
Zusammenfassung:
Sixty years ago, the first protein structure of myoglobin was determined by John Kendrew and his colleagues; hemoglobin followed shortly thereafter. For quite some time, it seemed that only X-ray crystallography would be capable of determining the structure of proteins to high resolution. In recent years, cryo-electron microscopy has emerged as a viable alternative and indeed in many cases the preferred approach. It is capable of studying proteins that span a size range from several megadaltons to proteins as small as myoglobin and hemoglobin. (C) 2017 Elsevier Ltd. All rights reserved.
