ライフサイエンスコーパス: cryo-EM

1 In 2013, cryo-EM and x-ray structures of soluble, cleaved SOSIP E

2 However, our recent 3D cryo-EM studies showed that the full-length p53 tetramer

3 A cryo-EM reconstruction of a soluble Env trimer bound to

4 A cryo-EM reconstruction of the ZM197M SOSIP.664 trimer co

5 A cryo-EM reconstruction of Vo from single-particle images

6 A cryo-EM structure of an APC/C-Cdh1 complex with Apc1(WD4

7 The 4.0 A cryo-EM structure of one of the most intricate enzyme sy

8 n addition to the crystal structures, a 15-A cryo-EM reconstruction reveals interdomain flexibility o

9 The 3.3-A cryo-EM structure of the 860-A-diameter isometric mutant

10 We used a 3.5-A cryo-EM reconstruction with imposed D7 symmetry to furth

11 The 3.6 A cryo-EM structure of a nascent chain-containing 60S-List

12 Here we present the 8 A cryo-EM structure of a soluble form of the poly-C9 compo

13 Here, we report a 6.9 A cryo-EM structure of F-actin complexed with the L253P AB

14 Biology, Heuer et al. (2017) present a 3.9-A cryo-EM structure of the 40S:ABCE1 post-splitting comple

15 rsible disassembly, we recently determined a cryo-EM reconstruction of yeast Vo The structure indicat

16 l procedure to derive an atomic model from a cryo-EM map with annotated metadata.

17 logy of direct electron counting to obtain a cryo-EM structure of human Ad5 at 3.2-A resolution.

18 he density map, analysis and annotation of a cryo-EM density map still primarily rely on fitting atom

19 of parameters influence the resolution of a cryo-EM structure.

20 Here, we present a cryo-EM structure of a hamster SUR1/rat Kir6.2 channel b

21 We present a cryo-EM structure of mouse Piezo1 in a closed conformati

22 Here we present a cryo-EM structure of the BamABCDE complex, at 4.9 A reso

23 Here we present a cryo-EM, 6.8-A resolution structure of an "immature" Chi

24 ce similarly, fit of stem atoms and fit to a cryo-EM density map.

25 Comparison with a cryo-EM map of the F1Fo monomer identifies subunits e an

26 In addition, cryo-EM can be used to observe electron-beam induced dis

27 Additional cryo-EM reconstructions of the virus-Fab complex for dif

28 This improved resolution will allow cryo-EM to make groundbreaking contributions in essentia

29 analysis, flexibility and hotspot analysis, cryo-EM flexible fitting, and transition pathway modelin

30 Yi et al. (2015) use biochemical assays and cryo-EM to determine the molecular architecture of an es

31 g a combinatorial approach of biophysics and cryo-EM.

32 onsistent with previous crystallographic and cryo-EM studies, the obtained force-extension curves on

33 negative-stain electron microscopy (EM) and cryo-EM showed twice as many high-SNR diffraction peaks,

34 is pointed out that single-molecule FRET and cryo-EM form natural complements in the characterization

35 ess in fluorescent technology, genetics, and cryo-EM.

36 ization, we used unmodified MamK protein and cryo-EM with helical 3D reconstruction in RELION to obta

37 structural determination approaches such as cryo-EM.

38 his 'high-exposure' technique should benefit cryo-EM work on all types of samples, especially those o

39 Comparisons between cryo-EM structures of Env trimer complexed with BG1 (6.2

40 llustrate the unique complementarity between cryo-EM and solution NMR for studies of molecular machin

41 avivirus antibodies with epitopes defined by cryo-EM or x-ray crystallography to assess the role of e

42 n high-resolution structure determination by cryo-EM and point to challenges that lie ahead.

43 reinitiation complex (PIC) was determined by cryo-EM and image processing at a resolution of 6-11 A.

44 -thiogalactopyranoside (PETG), determined by cryo-EM at an average resolution of ~2.2 angstroms (A).

45 for high-resolution structure elucidation by cryo-EM.

46 I1III2IV1 from bovine heart mitochondria by cryo-EM at 9 A resolution.

47 ility in the crenactin filaments observed by cryo-EM and helps to explain the variability in twist th

48 trical hexamer would appear as a pentamer by cryo-EM, a technology that acquires the average of many

49 The structure of gamma-secretase revealed by cryo-EM approaches suggested a substrate binding mechani

50 such channel, NOMPC, was recently solved by cryo-EM, revealing a bundle of helices that may act as c

51 e method to three systems recently solved by cryo-EM, we are able to improve model geometry while mai

52 the T. thermophilus V/A-ATPase structure by cryo-EM at 6.4 A resolution.

53 us to determine the 50-kDa Fab structure by cryo-EM.

54 ecular dynamics simulations and suggested by cryo-EM studies.

55 ssed in its ground state by determining ClpC cryo-EM structures with and without MecA.

56 Combining cryo-EM data with bioinformatic analysis allowed us to d

57 In contrast, cryo-EM structural analysis of the R141H mutation at app

58 s and Fab were fitted into the corresponding cryo-EM densities to identify the antigenic epitope.

59 Here we report the electron cryomicroscopic (cryo-EM) structure of the intact apoptosome from Drosoph

60 ere single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP syntha

61 Electron cryomicroscopy (cryo-EM) has been used to determine the atomic coordinat

62 Here, we present electron cryomicroscopy (cryo-EM) maps showing that VAT undergoes large conformat

63 We have used electron cryomicroscopy (cryo-EM) to examine the filaments formed by the protein

64 ransient process by electron cryomicroscopy (cryo-EM) to reveal the structure of the substrate-bound

65 Using electron cryomicroscopy (cryo-EM) we have structurally characterized at high reso

66 Using electron cryomicroscopy (cryo-EM), we present a reconstruction of a fibril formed

67 ides, determined by electron cryomicroscopy (cryo-EM).

68 owever, compared with X-ray crystallography, cryo-EM is a young technique with distinct challenges.

69 mation available from X-ray crystallography, cryo-EM methods can provide useful complementary insight

70 Here, we determined cryo-EM structures of CorA in the Mg(2+)-bound closed co

71 Using cutting-edge cryo-EM technology with electron counting, we improved t

72 f the FA targeted states, and place existing cryo-EM and crystal structures in their functional conte

73 f DeepEM to several challenging experimental cryo-EM datasets demonstrated its ability to avoid the s

74 y a faithful replication of the experimental cryo-EM map computed using the coordinates and associate

75 ns IIIa, VIII, and IX from conventional/film cryo-EM and X-ray crystallography studies have caused co

76 Here we report the first cryo-EM structure of ATM kinase, which is an intact homo

77 RELION was originally developed for cryo-EM single-particle analysis, and the subtomogram av

78 may offer a viable computing environment for cryo-EM.

79 rted an in-focus data acquisition method for cryo-EM single-particle analysis with the Volta phase pl

80 are similar in the frozen specimens used for cryo-EM and in the solution phase where NMR spectra are

81 We report four cryo-EM structures of E. coli RelA bound to the 70S ribo

82 tly proposed "tunnel mechanism" of CETP from cryo-EM studies for the transfer of neutral lipids betwe

83 Taken together, the data from cryo-EM and flow cytometry argue that Bax promotes MOMP

84 utomatic recognition of particle images from cryo-EM micrographs.

85 completion of macromolecular structures from cryo-EM density maps at 3-5-A resolution.

86 Here, cryo-EM and biochemistry show that the human E3 anaphase

87 es we have gained through recent advances in cryo-EM.

88 and presents a major practical bottleneck in cryo-EM structural determination.

89 The recent developments in cryo-EM have revolutionized our access to previously ref

90 akes 5-15 d for an individual experienced in cryo-EM.

91 upancy and binding stoichiometry observed in cryo-EM, without having to account for differences in ep

92 e performed beyond that recently reported in cryo-EM models provide structural insights that may be u

93 o facilitate modeling of macromolecules into cryo-EM density maps, fast and easy to use methods for m

94 tein segments can be accurately modeled into cryo-EM density maps of different resolution by FragFit.

95 flexible protein parts or hinge-regions into cryo-EM density maps.

96 based approach for modeling of segments into cryo-EM density maps (termed FragFit).

97 of known or modeled protein structures into cryo-EM density maps.

98 most computationally intensive steps of its cryo-EM structure determination workflow.

99 resource that may be limiting to many likely cryo-EM users.

100 ecent studies using cryo-electron microcopy (cryo-EM), computational analysis, and functional quantif

101 from one area of a cryo-electron microscope (cryo-EM) specimen grid to another, from one grid to the

102 We determined electron cryo-microscopy (cryo-EM) and crystal structures of unbound and H1-bound

103 in single-particle electron cryo-microscopy (cryo-EM) data processing allowing for the rapid determin

104 Although electron cryo-microscopy (cryo-EM) has recently achieved resolutions of better tha

105 a series of tilted electron cryo-microscopy (cryo-EM) images.

106 rticle analysis of electron cryo-microscopy (cryo-EM) is a key technology for elucidation of macromol

107 Single-particle electron cryo-microscopy (cryo-EM) is an emerging tool for resolving structures of

108 atomic resolution electron cryo-microscopy (cryo-EM) structure of the Leishmania ribosome in complex

109 bound to ICP47 by electron cryo-microscopy (cryo-EM) to 4.0 A.

110 o, single-particle electron cryo-microscopy (cryo-EM) was usually not the first choice for many struc

111 s in single-particle cryoelecton microscopy (cryo-EM) are enabling generation of numerous near-atomic

112 Here, we present cryoelectron microscopy (cryo-EM) maps of 80SCrPV-STOP eRF1 eRF3 GMPPNP and 80SCr

113 In addition, cryoelectron microscopy (cryo-EM) reconstructions of virion capsids did not detec

114 ere, we present the cryoelectron microscopy (cryo-EM) structure of a KCNQ1/calmodulin (CaM) complex.

115 Here, we use cryoelectron microscopy (cryo-EM) to determine the quaternary structure of an act

116 meter resolution by cryoelectron microscopy (cryo-EM), showed only four proteins per icosahedral asym

117 Using cryoelectron microscopy (cryo-EM), we show that the binding of target double-stra

118 by single-particle cryo-electron microscopy (cryo-EM) and allowed us to stabilize the HIV envelope gl

119 Based on cryo-electron microscopy (cryo-EM) and dynamic light scattering (DLS) alpha-Syn li

120 ng single-particle cryo-electron microscopy (cryo-EM) and image classification to samples in the pres

121 ter ejection using cryo-electron microscopy (cryo-EM) and single particle reconstruction methods reve

122 e obtained by cryogenic electron microscopy (cryo-EM) and single-particle analysis.

123 photographic film cryo-electron microscopy (cryo-EM) and X-ray crystallography studies, but discrepa

124 of single particle cryo-electron microscopy (cryo-EM) as a technique to generate high-resolution stru

125 ensitized state by cryo-electron microscopy (cryo-EM) at 3.8 A resolution, we show that desensitizati

126 e demonstrate that cryo-electron microscopy (cryo-EM) can be used to image nanoscale lipid and polyme

127 Cryo-electron microscopy (cryo-EM) had played a central role in the study of ribos

128 Single-particle cryo-electron microscopy (cryo-EM) has become a mainstream tool for the structural

129 ch single-particle cryo-electron microscopy (cryo-EM) has emerged as a method for determining high-re

130 wever, progress in cryo-electron microscopy (cryo-EM) has made possible the visualization, at increas

131 Fab) was solved by cryo-electron microscopy (cryo-EM) image reconstruction.

132 Cryo-electron microscopy (cryo-EM) is a powerful technique for the modeling of pro

133 3D cryo-electron microscopy (cryo-EM) is an expanding structural biology technique th

134 Cryo-electron microscopy (cryo-EM) is rapidly emerging as a powerful tool for prot

135 Here we present cryo-electron microscopy (cryo-EM) maps at 3.4-3.5 A resolution and corresponding

136 ar structures into cryo-electron microscopy (cryo-EM) maps is a major challenge, as the moderate reso

137 rt high resolution cryo electron microscopy (cryo-EM) maps of wild type CPMV containing RNA-2, and of

138 -atomic-resolution cryo-electron microscopy (cryo-EM) maps.

139 Cryo-electron microscopy (cryo-EM) methods are now being used to determine structu

140 rids, we performed cryo-electron microscopy (cryo-EM) of His6-GroEL obtained from clarified E. coli l

141 Cryo-electron microscopy (cryo-EM) of single-particle specimens is used to determi

142 Cryo-electron microscopy (cryo-EM) reconstruction at subnanometer resolution revea

143 nt single particle cryo-electron microscopy (cryo-EM) reconstructions of 48S PICs from yeast in these

144 olution (3.9-4.2A) cryo-electron microscopy (cryo-EM) reconstructions of MTs stabilized by the taxane

145 e, we present five cryo-electron microscopy (cryo-EM) reconstructions of ribosomes purified from P. f

146 in high-resolution cryo-electron microscopy (cryo-EM) require the development of validation metrics t

147 c configuration by cryo-electron microscopy (cryo-EM) since the contact by the arginine finger render

148 Combining cryo-electron microscopy (cryo-EM) structure analysis and biochemical approaches,

149 e report the 4.2-A cryo-electron microscopy (cryo-EM) structure and in vitro dynamics parameters of a

150 resolution (8.5-A) cryo-electron microscopy (cryo-EM) structure of a chimeric VLP and developed a VP1

151 present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks o

152 ere we present the cryo-electron microscopy (cryo-EM) structure of a full-length TRPML3 channel from

153 a high-resolution cryo-electron microscopy (cryo-EM) structure of the core tetrameric HIV-1 STC and

154 ere, we report the cryo-electron microscopy (cryo-EM) structure of the Csy complex bound to two diffe

155 Here we present cryo-electron microscopy (cryo-EM) structures at 3.5-3.8 A resolution of mammalian

156 We report cryo-electron microscopy (cryo-EM) structures for adenosine diphosphate (ADP)-boun

157 The cryo-electron microscopy (cryo-EM) structures of a mature HPV16 particle and an al

158 We determined the cryo-electron microscopy (cryo-EM) structures of HMAb 2D22 complexed with two diff

159 We report six cryo-electron microscopy (cryo-EM) structures of MTs, at 3.5 A or better resolutio

160 ere, we report the cryo-electron microscopy (cryo-EM) structures of Qbeta with and without symmetry a

161 gh-resolution cryogenic electron microscopy (cryo-EM) structures of ribosomes proliferate, at resolut

162 staining (NS) and cryo-electron microscopy (cryo-EM) suggest that this method has a comparable capab

163 iruses analyzed by cryo-electron microscopy (cryo-EM) to date.

164 mechanism, we used cryo-electron microscopy (cryo-EM) to visualize Bax-induced pores in purified mito

165 rrelated cryo-fLM, cryo-electron microscopy (cryo-EM), and cryo-ET (i.e., cryo-CLEM) of virus-infecte

166 We report cryo-electron microscopy (cryo-EM), biophysical, biochemical, and cell biological

167 In single-particle cryo-electron microscopy (cryo-EM), molecules suspended in a thin aqueous layer ar

168 y binding studies, cryo-electron microscopy (cryo-EM), mutational analyses, peptide binding analysis,

169 ng single-particle cryo-electron microscopy (cryo-EM), reveal structural details that help explain th

170 rapid progress in cryo-electron microscopy (cryo-EM), there still exist ample opportunities for impr

171 s been moot as, in cryo-electron microscopy (cryo-EM), they would be camouflaged by the surrounding D

172 recent advances in cryo-electron microscopy (cryo-EM), we determined the structure of CPV in complex

173 nts from ssNMR and cryo-electron microscopy (cryo-EM), we establish an atomic resolution model of the

174 Previously, using cryo-electron microscopy (cryo-EM), we showed that activated Bax forms large, grow

175 rus, determined by cryo-electron microscopy (cryo-EM).

176 y single-particle, cryo-electron microscopy (cryo-EM).

177 ate resolutions by cryo-electron microscopy (cryo-EM).

178 determined by cryogenic electron microscopy (cryo-EM).

179 Cryo-electron-microscopy (cryo-EM) structures of flaviviruses reveal significant v

180 gle-particle cryogenic electron microscopy ("cryo-EM"), for example, large datasets are required for

181 Here we use cryo-electron microscropy (cryo-EM) to determine near-atomic resolution structures

182 l model of Hsp21 based on homology modeling, cryo-EM, cross-linking mass spectrometry, NMR, and small

183 strates that a force field is not necessary, cryo-EM data alone is sufficient to accurately guide the

184 By integrating NMR, cryo-EM, and molecular dynamics simulations, we show tha

185 , for single-particle recognition from noisy cryo-EM micrographs, enabling automated particle picking

186 A novel adaptation of cryo-EM based on detecting gas bubbles generated by radi

187 y has taken advantage of new capabilities of cryo-EM, in visualizing several structures co-existing i

188 lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography.

189 The procedure optimizes contrast of cryo-EM densities by amplitude scaling against the radia

190 ct complexes from the detrimental effects of cryo-EM sample preparation.

191 n, significantly improving the efficiency of cryo-EM data processing.

192 h we can rightly celebrate the maturation of cryo-EM as a high-resolution structure-determination too

193 er may result in more reliable production of cryo-EM specimens with the desired thickness.

194 nts significantly enhanced the resolution of cryo-EM density maps and broadened the applicability and

195 ctors has greatly improved the resolution of cryo-EM structures to the point where atomic resolution

196 a general procedure for local sharpening of cryo-EM density maps based on prior knowledge of an atom

197 This study demonstrates the utility of cryo-EM in revealing structure dynamics within a single

198 rs present the CVA6 procapsid and A-particle cryo-EM structures and identify an immune-dominant neutr

199 s of specimen orientation in single particle cryo-EM and present open-source software for rapidly ass

200 Using a 2.6 A resolution single particle cryo-EM reconstruction of rotavirus VP6, determined from

201 pore structure of lysenin by single particle cryo-EM, to 3.1 A resolution.

202 s, two perceived barriers in single-particle cryo-EM are overcome: (1) crossing 2 A resolution and (2

203 er forms, were determined by single-particle cryo-EM at 3.9 A and 5.6 A, respectively.

204 Here, we describe a 3.6 A single-particle cryo-EM reconstruction of the core CBF3 complex, incorpo

205 r a wide range of specimens, single-particle cryo-EM structure determination is transforming structur

206 Nearly all single-particle cryo-EM structures resolved to better than 4-A resolutio

207 n structure determination by single-particle cryo-EM to provide an overview for scientists wishing to

208 zi ribosome large subunit by single-particle cryo-EM.

209 solutions close to 2 A using single-particle cryo-EM.

210 ins, SpoIIIAG, determined by single-particle cryo-EM.

211 Here, we present cryo-EM reconstructions of RyR1 in multiple functional s

212 Here, we present cryo-EM structures of Drp1 helices on nanotubes with dis

213 We present cryo-EM structures of E. coli RNAP core bound to the sma

214 Here we present cryo-EM structures of EVN and AVI in complex with the Es

215 Here we present cryo-EM structures of the unique minus-end directed myos

216 confirmed the main conclusions from previous cryo-EM at lower resolution, including the association o

217 tructure unambiguously confirms our previous cryo-EM models of proteins IIIa, VIII, and IX and explai

218 llows automated particle extraction from raw cryo-EM micrographs in the absence of a template.

219 Recent cryo-EM structures of the Mcm2-7 (MCM) double hexamer, i

220 Recent cryo-EM studies revealed detailed channel structures, op

221 A recent cryo-EM structure of a native full-length trimer without

222 A recent cryo-EM study of holo V-ATPase revealed three major conf

223 l structural elements not detected in recent cryo-EM reconstructions of RyRs.

224 Until recently cryo-EM structures were limited to approximately 10 A in

225 We also report cryo-EM structures (at resolutions of ~3.3, 3.2, and 3.3

226 Here, we report cryo-EM structures of an AMPAR in complex with the auxil

227 In addition, analysis of a 10 A resolution cryo-EM map of an empty prolate T4 head shows how the do

228 ectrometry analysis and the 5-6 A resolution cryo-EM maps of the 45SYphC and 44.5SYsxC particles reve

229 We report a 4.3 A resolution cryo-EM structure of the active Vps4 hexamer with its co

230 Building upon our earlier 4.3 A resolution cryo-EM structure, we now report a 3.2 A structure of Vp

231 We report two 3.2 A resolution cryo-EM structures - determined from a single sample - o

232 Here, we present 3.8 A resolution cryo-EM structures of the cancer target isocitrate dehyd

233 Here we describe a 4-A-resolution cryo-EM structure of monomeric PRC1 bound to MTs.

234 Here we present near-atomic resolution cryo-EM structures for flagellar filaments from both Gra

235 e the authors present near-atomic resolution cryo-EM structures of nine flagellar filaments, and begi

236 Here, we report near-atomic resolution cryo-EM structures, at resolutions ranging from 3.2 A to

237 are manually built in near-atomic-resolution cryo-EM maps.

238 However, high-resolution cryo-EM reconstruction often requires hundreds of thousa

239 ed compounds and present the high-resolution cryo-EM structural analysis of the human immunoproteasom

240 This enables high-resolution cryo-EM structure determination in a matter of days on a

241 We provide a high-resolution cryo-EM structure of a virus-ICAM-1 complex, which revea

242 laboratories could determine high-resolution cryo-EM structures for $50 to $1500 per structure within

243 Therefore, even very low resolution cryo-EM data is superior in predicting heterodimeric and

244 At low resolution, cryo-EM maps can drive integrative modeling of the inter

245 rTRPV1 cryo-EM structures implicated rotation of this residue i

246 By testing the procedure using six cryo-EM structures of TRPV1, beta-galactosidase, gamma-s

247 Using the recently solved cryo-EM structure for the Eag-family channel as a templa

248 structure agrees well with a recently solved cryo-EM structure of a CFTR IWF state.

249 ssure) can hardly be avoided during standard cryo-EM specimen preparation.

250 n pathway modeling) based on an active-state cryo-EM map.

251 These findings demonstrate that cryo-EM allows atomic characterization of amyloid filame

252 Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general

253 ins with sizes < 100 kDa, demonstrating that cryo-EM can be used to investigate a broad spectrum of d

254 review, we summarize important insights that cryo-EM, in combination with chemical and genetic approa

255 The cryo-EM reconstruction suggests a parallel orientation o

256 The cryo-EM structure of one chimeric VLP (Yokote/Mc114) was

257 The cryo-EM structure of the closed state reveals an ordered

258 The cryo-EM structure revealed that the P domain dimers were

259 The cryo-EM studies disagree on the position of SPRY domains

260 Although the cryo-EM structures resolved the conundrum of whether mam

261 e underlie some of the principles behind the cryo-EM methodology of single particle analysis and disc

262 This is supported by the cryo-EM reconstruction of P22 mature virion tail, where

263 ext of the mature subunit, we determined the cryo-EM structure of the fully assembled 30S subunit in

264 Here, we determined the cryo-EM structures of chikungunya virus-like particles c

265 igin activation, here we have determined the cryo-EM structures of DNA-bound MCM, either unmodified o

266 h this residue, which is recognizable in the cryo-EM electron density, may function as an attachment

267 Based on the orientation of capsomers in the cryo-EM reconstruction, we propose that the capsids of C

268 ovel fold, which is largely invisible in the cryo-EM structure of the HKU1 S trimer.

269 odel of the PilQ protein was fitted into the cryo-EM map.

270 tting of the VP90(71-415) structure into the cryo-EM maps of HAstV produced an atomic model for the T

271 human FANCD2-FANCI complex by obtaining the cryo-EM structure.

272 Our analysis of the cryo-EM reconstructions of the HPV16 capsids and virus-F

273 Analysis of the cryo-EM spliceosome B(act) complex shows that the resist

274 density maps are the ultimate result of the cryo-EM structure determination process.

275 Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to t

276 Here, we present the cryo-EM structure of PKD2 in lipid bilayers at 3.0 A res

277 Here, we present the cryo-EM structure of the entire SAGA complex where the m

278 Here, we present the cryo-EM structure of this bifunctional complex at a reso

279 Here, we report the cryo-EM atomic structures of the full virion and native

280 Here, Wang et al. report the cryo-EM structure of mature JEV at near-atomic resolutio

281 Here, we report the cryo-EM structure of the Mcm2-7 DH on dsDNA and show tha

282 At 4.1 A resolution, the cryo-EM structure of the Dark apoptosome bound to the ca

283 The method should streamline the cryo-EM structure determination process, providing accur

284 Here, we report for the first time the cryo-EM structure and in vitro dynamics parameters of re

285 s can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just

286 Therefore, cryo-EM can be used to investigate complete and fully fu

287 These cryo-EM structures establish the sequence of nucleotide-

288 onolayer at the air-water interface of thin, cryo-EM specimens has been largely underappreciated.

289 Here we present two cryo-EM snapshots of the Thermobifida fusca type I-E Cas

290 Here we use cryo-EM reconstruction techniques to solve the structure

291 We have used cryo-EM single-particle 3D reconstruction to solve the s

292 Here, we have used cryo-EM to elucidate the sRNA orientation in a M. jannas

293 Here, we used cryo-EM to elucidate structural basis of channel assembl

294 Here we used cryo-EM to show that gold-labeled Bax molecules, after a

295 We used cryo-EM to study a heterogeneous population of SBPV viri

296 Using cryo-EM, we have been able to generate a nearly complete

297 Using cryo-EM, we show that the membrane in AFV1 is a 2 nm-th

298 More extensive studies, using cryo-EM methodology, of translation in the parasite will

299 Whether cryo-EM methods are equally useful for high-resolution s

300 By combining hybrid mass spectrometry with cryo-EM, computational and biochemical data, we investig