5NI1
CryoEM structure of haemoglobin at 3.2 A determined with the Volta phase plate
「5ME2」から置き換えられました5NI1 の概要
| エントリーDOI | 10.2210/pdb5ni1/pdb |
| EMDBエントリー | 3488 |
| 分子名称 | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| 機能のキーワード | volta phase plate, single particle analysis, hemoglobin, oxygen transport |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 64547.05 |
| 構造登録者 | Khoshouei, M.,Radjainia, M.,Bunker, R.,Baumeister, W.,Danev, R. (登録日: 2017-03-22, 公開日: 2017-04-12, 最終更新日: 2024-05-08) |
| 主引用文献 | Khoshouei, M.,Radjainia, M.,Baumeister, W.,Danev, R. Cryo-EM structure of haemoglobin at 3.2 angstrom determined with the Volta phase plate. Nat Commun, 8:16099-16099, 2017 Cited by PubMed Abstract: With the advent of direct electron detectors, the perspectives of cryo-electron microscopy (cryo-EM) have changed in a profound way. These cameras are superior to previous detectors in coping with the intrinsically low contrast and beam-induced motion of radiation-sensitive organic materials embedded in amorphous ice, and hence they have enabled the structure determination of many macromolecular assemblies to atomic or near-atomic resolution. Nevertheless, there are still limitations and one of them is the size of the target structure. Here, we report the use of a Volta phase plate in determining the structure of human haemoglobin (64 kDa) at 3.2 Å. Our results demonstrate that this method can be applied to complexes that are significantly smaller than those previously studied by conventional defocus-based approaches. Cryo-EM is now close to becoming a fast and cost-effective alternative to crystallography for high-resolution protein structure determination. PubMed: 28665412DOI: 10.1038/ncomms16099 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
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