EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Below 3 Å structure of apoferritin using a multipurpose TEM with a side entry cryoholder.
ジャーナル・号・ページ	Sci Rep, Vol. 11, Issue 1, Page 8395, Year 2021
掲載日	2021年4月16日
著者	Yoko Kayama / Raymond N Burton-Smith / Chihong Song / Naoya Terahara / Takayuki Kato / Kazuyoshi Murata /
PubMed 要旨	Recently, the structural analysis of protein complexes by cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has had great impact as a biophysical method. Many results of cryo-EM SPA ...Recently, the structural analysis of protein complexes by cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has had great impact as a biophysical method. Many results of cryo-EM SPA are based on data acquired on state-of-the-art cryo-electron microscopes customized for SPA. These are currently only available in limited locations around the world, where securing machine time is highly competitive. One potential solution for this time-competitive situation is to reuse existing multi-purpose equipment, although this comes with performance limitations. Here, a multi-purpose TEM with a side entry cryo-holder was used to evaluate the potential of high-resolution SPA, resulting in a 3 Å resolution map of apoferritin with local resolution extending to 2.6 Å. This map clearly showed two positions of an aromatic side chain. Further, examination of optimal imaging conditions depending on two different multi-purpose electron microscope and camera combinations was carried out, demonstrating that higher magnifications are not always necessary or desirable. Since automation is effectively a requirement for large-scale data collection, and augmenting the multi-purpose equipment is possible, we expanded testing by acquiring data with SerialEM using a β-galactosidase test sample. This study demonstrates the possibilities of more widely available and established electron microscopes, and their applications for cryo-EM SPA.
リンク	Sci Rep / PubMed:33863933 / PubMed Central
手法	EM (単粒子)
解像度	3.0 - 5.1 Å
構造データ	EMDB-30095: 3.6A beta-galactosidase using JEM-2100F + K2 Summit, SerialEM acquisition, RELION 3.0 processing. 手法: EM (単粒子) / 解像度: 3.6 Å EMDB-30096: 3A Apoferritin, JEM-2100F + K2 Summit, 50K, RELION 3.1 手法: EM (単粒子) / 解像度: 3.0 Å EMDB-30097: 3.3A apoferritin from JEM-2100F + K2 Summit at 50K with symmetry expansion. 手法: EM (単粒子) / 解像度: 3.3 Å EMDB-30098: 3.3A apoferritin from JEM-2100F + K2 Summit at 50K with octahedral symmetry. 手法: EM (単粒子) / 解像度: 3.3 Å EMDB-30099: 3.9A apoferritin from JEM-2100F + K2 Summit at 60K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 3.9 Å EMDB-30100: 3.4A apoferritin from JEM-2100F + K2 Summit at 40K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 3.4 Å EMDB-30101: 4A apoferritin from JEM-2100F + K2 Summit at 30K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-30103: 4.5A apoferritin from JEM-2200FS + DE-20 at 40K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 4.5 Å EMDB-30105: 3.8A apoferritin from JEM-2200FS + DE-20 at 60K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 3.8 Å EMDB-30106: 3.9A apoferritin from JEM-2200FS + DE-20 at 80K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 3.9 Å EMDB-30107: 5.1A apoferritin from JEM-2200FS + DE-20 at 100K, RELION 3.0 processing, manual acquisition. 手法: EM (単粒子) / 解像度: 5.1 Å
由来	Escherichia coli (大腸菌) Mus musculus (ハツカネズミ)