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1 X-ray crystallography, NMR spectroscopy, and cryo electron microscopy.
2 NA to 3.8 A resolution using single-particle cryo-electron microscopy.
3 s complex at 3.6-A resolution, determined by cryo-electron microscopy.
4 ORC determined by X-ray crystallography and cryo-electron microscopy.
5 -220 A diameter mini-rings, here observed by cryo-electron microscopy.
6 molecules was determined by single-particle cryo-electron microscopy.
7 mmalian (ovine) supercomplexes determined by cryo-electron microscopy.
8 o 3.9-angstrom resolution by single-particle cryo-electron microscopy.
9 gth TRPV2 at approximately 5 A resolution by cryo-electron microscopy.
10 sions to be high fidelity by single-particle cryo-electron microscopy.
11 coli F-ATP synthase has been generated using cryo-electron microscopy.
12 1 S protein determined using single-particle cryo-electron microscopy.
13 rtaker in the blooming of a technique I love-cryo-electron microscopy.
14 mined at 4.0 A resolution by single particle cryo-electron microscopy.
15 resolution, as determined by single-particle cryo-electron microscopy.
16 of the active human apoptosome determined by cryo-electron microscopy.
17 odel of the CVB3-DAF interaction obtained by cryo-electron microscopy.
18 tracted Vibrio cholerae sheath determined by cryo-electron microscopy.
19 sents a significant technical advance for 3D cryo-electron microscopy.
20 of Pvr at a 4-A resolution, as determined by cryo-electron microscopy.
21 OS-1 antibody Fab fragment was determined by cryo-electron microscopy.
22 n bound to lipid nanotubes, as determined by cryo-electron microscopy.
23 S. cerevisiae Pol II-Rad26 complex solved by cryo-electron microscopy.
24 and the complete Mtb 70S ribosome, solved by cryo-electron microscopy.
25 employing time-resolved x-ray scattering and cryo-electron microscopy.
26 ermined by Volta phase-plate single-particle cryo-electron microscopy.
27 recipitation experiments and single particle cryo-electron microscopy.
28 e molecular structure of hERG to 3.8 A using cryo-electron microscopy.
29 tructure of a WRC-Rac1 complex determined by cryo-electron microscopy.
30 d two tissue culture adapted FMDV strains by cryo-electron microscopy.
31 ECs) with and without Nun by single-particle cryo-electron microscopy.
32 ucture of a bovine CLC channel (CLC-K) using cryo-electron microscopy.
33 ffraction or NMR data), and 3D reconstructed cryo-electron microscopy (3D EM) maps (albeit at coarser
34 with stem-specific monoclonal antibodies and cryo-electron microscopy analysis of HA-SS on ferritin n
36 WV determined to a resolution of 3.1 A using cryo-electron microscopy and 3.8 A by X-ray crystallogra
37 structure determination of mouse TMEM16A by cryo-electron microscopy and a complementary functional
42 plex (Med-PIC) was assembled and analyzed by cryo-electron microscopy and by chemical cross-linking a
45 b, AAV5-ADK5a, and AAV5-ADK5b, determined by cryo-electron microscopy and image reconstruction to a r
51 20S proteasome bound to the inhibitor using cryo-electron microscopy and single-particle analysis, t
52 the stabilized mutant at 3.6 A resolution by cryo-electron microscopy and single-particle reconstruct
53 o motility assays, single-molecule tracking, cryo-electron microscopy and structural probing (16) .
54 etermined to a resolution of 2.8 to 3.0 A by cryo-electron microscopy and three-dimensional image rec
55 ent variant, AAV2-R432A, were examined using cryo-electron microscopy and three-dimensional image rec
56 2, HBoV1-9G12, and HBoV1-12C1, determined by cryo-electron microscopy and three-dimensional image rec
57 mined using X-ray crystallography as well as cryo-electron microscopy and three-dimensional image rec
59 ly analyze their subcellular water states by cryo-electron microscopy and tomography, cryoelectron di
60 and Esigma(70) determined by single-particle cryo-electron microscopy and validation of the structure
61 ding motif (MBM) assembling around MTs using cryo-electron microscopy and verified it with chemical c
65 e results of others that were obtained using cryo-electron microscopy (and single particle analysis),
67 0 approximately Ub-substrate intermediate by cryo-electron microscopy, and in isolation by X-ray crys
68 type CHIKV, as determined by single-particle cryo-electron microscopy, and it mimicked the early stag
69 methods, including atomic force microscopy, cryo-electron microscopy, and neutron scattering, to inv
70 aPI1 procapsids to near-atomic resolution by cryo-electron microscopy, and show that CpmB competes wi
72 ctron microscopy of frozen hydrated samples (cryo-electron microscopy) are providing unprecedented op
73 e isolated lid sub-complex, as determined by cryo-electron microscopy at 3.5 A resolution, revealing
74 lizer, was constructed, and its structure by cryo-electron microscopy at 6.2 A resolution reveals a c
75 o2.2, in the Na(+)-free state, determined by cryo-electron microscopy at a nominal resolution of 4.5
77 promoter DNA, determined by single-particle cryo-electron microscopy at sub-nanometre resolution.
80 -ray crystallography, homology modeling, and cryo-electron microscopy by an integrative modeling appr
81 alyzed by a hybrid structural approach using cryo-electron microscopy, chemical cross-linking coupled
84 tide transporter PeptTSo2 by single-particle cryo-electron microscopy (cryo-EM) and allowed us to sta
87 ation of the phage tail after ejection using cryo-electron microscopy (cryo-EM) and single particle r
88 derived independently from photographic film cryo-electron microscopy (cryo-EM) and X-ray crystallogr
89 as realized the potential of single particle cryo-electron microscopy (cryo-EM) as a technique to gen
90 r GluK2 subtype in its desensitized state by cryo-electron microscopy (cryo-EM) at 3.8 A resolution,
94 The suddenness with which single-particle cryo-electron microscopy (cryo-EM) has emerged as a meth
95 In the last few years, however, progress in cryo-electron microscopy (cryo-EM) has made possible the
96 U4 fragments of antibody (Fab) was solved by cryo-electron microscopy (cryo-EM) image reconstruction.
100 c modeling of macromolecular structures into cryo-electron microscopy (cryo-EM) maps is a major chall
103 orkflow enabled by these grids, we performed cryo-electron microscopy (cryo-EM) of His6-GroEL obtaine
105 We have obtained high-resolution (3.9-4.2A) cryo-electron microscopy (cryo-EM) reconstructions of MT
108 ly reported as a pentameric configuration by cryo-electron microscopy (cryo-EM) since the contact by
111 etermined an intermediate-resolution (8.5-A) cryo-electron microscopy (cryo-EM) structure of a chimer
113 , through which we present a high-resolution cryo-electron microscopy (cryo-EM) structure of the core
121 lidations by both negative staining (NS) and cryo-electron microscopy (cryo-EM) suggest that this met
123 To resolve aspects of the mechanism, we used cryo-electron microscopy (cryo-EM) to visualize Bax-indu
124 scribe our protocol for correlated cryo-fLM, cryo-electron microscopy (cryo-EM), and cryo-ET (i.e., c
127 such as data from antibody binding studies, cryo-electron microscopy (cryo-EM), mutational analyses,
128 d CFTR), determined by using single-particle cryo-electron microscopy (cryo-EM), reveal structural de
130 l proteins in C capsids has been moot as, in cryo-electron microscopy (cryo-EM), they would be camouf
137 atomic model of the archaella, based on the cryo electron microscopy (cryoEM) structure of the Metha
138 ly confirm the identity of this T6SS and, by cryo electron microscopy (cryoEM), show the structure of
139 resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconst
140 software have revolutionized single particle cryo-electron microscopy (cryoEM) and led to a wave of n
141 probe their molecular architectures by using cryo-electron microscopy (cryoEM) image reconstruction t
143 present a 6.2 A resolution three-dimensional cryo-electron microscopy (cryoEM) structure of an infect
144 ucture of the CVB3-DAF complex determined by cryo-electron microscopy, DAF S104 is in close contact w
145 h as several NMR observables, FRET, SAXS and cryo-electron microscopy data, and enables modelling str
146 litated 3D helical image reconstruction from cryo-electron microscopy data, revealing the basic tube
147 Coarse-grained models are compared with 3D cryo-electron microscopy density maps for these five DNA
149 s, characterized by atomic force microscopy, cryo-electron microscopy, dynamic light scattering, and
150 n NMR, these nanodiscs can also be used for (cryo-) electron microscopy (EM) and small-angle X-ray an
151 tting of the VP90(71-415) structure into the cryo-electron microscopy (EM) maps of HAstV produced an
152 paradigm, are presented that resolve sub-5 A cryo-electron microscopy (EM) maps with either single st
161 Three-dimensional reconstruction based on cryo-electron microscopy images and single-particle imag
163 re collected for each selected crystal using cryo-electron microscopy, in which the crystal is diffra
164 sional reconstruction of images generated by cryo-electron microscopy indicates that the SpoIIIAG rin
167 , elucidated at near-atomic resolution using cryo-electron microscopy, is strikingly similar to that
168 ) was recently modeled in our 9 A resolution cryo-electron microscopy map by fitting protein and TER
173 ing protein structure models on the basis of cryo-electron microscopy maps with near-atomic resolutio
174 structures of this segment determined by the cryo-electron microscopy method micro-electron diffracti
176 equilibrium constant measurements as well as cryo-electron microscopy methodologies to investigate th
178 ray scattering, free-electron laser imaging, cryo-electron microscopy, nuclear magnetic resonance, el
180 erized, RNA-encapsidating nucleoprotein, and cryo-electron microscopy of nucleocapsid or nucleocapsid
185 -bound subunit PulG into the 5-A-resolution cryo-electron microscopy reconstruction of assembled fib
187 dis major pilin PilE and a approximately 6 A cryo-electron microscopy reconstruction of the intact pi
196 In this study, we present high-resolution cryo-electron microscopy reconstructions of poliovirus w
197 s spectrometric analysis and single-particle cryo-electron microscopy reconstructions of the BtAdV 25
199 tative mass spectrometry and single-particle cryo-electron microscopy reveal 13 distinct intermediate
202 olysaccharide profiles, protein profiles and cryo-electron microscopy revealed that there were no sig
208 n p53/Pol II interaction via single-particle cryo-electron microscopy, structural docking, and bioche
209 etermination of intact human gamma-secretase cryo-electron microscopy structure has opened the way fo
210 oreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramat
216 Here we present, at 3.8 A resolution, the cryo-electron microscopy structure of a Saccharomyces ce
231 product integration complexes, as well as a cryo-electron microscopy structure of the full CRISPR lo
242 A comparison with the recently determined cryo-electron microscopy structure of the U4/U6.U5 tri-s
247 -molecule biochemistry, our hybrid X-ray and cryo-electron microscopy structure of TTLL7 bound to the
248 ffect vector transmission, we determined the cryo-electron microscopy structure of wild-type CNV in t
250 Using a model substrate (casein), we report cryo-electron microscopy structures at near-atomic resol
252 croscopy have resulted in a series of atomic cryo-electron microscopy structures of both human and ye
254 mparisons of six high-resolution (2.9-3.1 A) cryo-electron microscopy structures of cytoplasmic polyh
260 de inserts into the channel is uncertain, as cryo-electron microscopy structures of the active channe
263 he major capsid protein, in combination with cryo-electron microscopy structures of two different mat
266 the structure of one of these conformers by cryo electron microscopy to near-atomic resolution, eluc
276 oquine and demonstrate the vast potential of cryo-electron microscopy to guide the development of mef
280 To understand this discrimination, we used cryo-electron microscopy to solve structures of Drosophi
281 Our previous paper used high-resolution cryo-electron microscopy to solve the structure of the E
283 in the transmembrane region of the original cryo-electron microscopy Torpedo model; the only pentame
286 hrough direct comparison with the results of cryo-electron microscopy, we demonstrate de novo reconst
296 d on these findings and structural data from cryo-electron microscopy, we suggest a refined disassemb
297 rAB from Vibrio alginolyticus, determined by cryo-electron microscopy, which, combined with EPR spect
298 ial complex I at 3.9 A resolution, solved by cryo-electron microscopy with cross-linking and mass-spe
300 basal body, determined using single-particle cryo-electron microscopy, with the inner-membrane-ring a
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