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1
Some residues move as much as 14Å in the process.
2
The HicABS crystal diffracted and data were collected to 2.5 Å resolution.
3
X-ray diffraction data were collected to 1.90 Å resolution using a synchrotron-radiation source.
4
Here, we describe the structure of the SAFs determined to approximately 8 Å resolution using cryotransmission electron microscopy.
5
Here we detail the 2.35 Å structure of ChoKa in complex with TCD-717.
6
The crystal structure of StSOR was determined at 1.73 Å resolution.
7
The 7.4 Å structure has only one similarly bound insulin per receptor dimer.
8
Here we determined the cryo-electron microscopy structure of human mTORC1 at 4.4 Å resolution.
9
Crystal structures of these complexes were determined at 2.7, 1.9 and 1.6 Å resolutions.
10
In this study, we present the X-ray crystal structure of AlgX at 2.15 Å resolution.
11
Searching for structural differences, the crystal structure of Fe-SODA was solved at 2.2 Å resolution.
12
Expanding the accessible range for FRET to 150 Å would open up many cellular interactions to fluorescence and fluorescence-lifetime imaging.
13
Secondary structures are confusing at 3-4 Å but can be better recognized at 6-8 Å.
14
The FSB's independence is enabled by the continuous water layer (greater than 15 Å) that remains between the two.
15
The MCNR studies provided structural resolution down to 1 Å, enabling accurate measurement of protein domains projecting from the membrane layer.
16
The cryo-EM structure was determined at 2.24 Å resolution using an instrument operating at 200 kV.