6MTG
A Single Reactive Noncanonical Amino Acid is Able to Dramatically Stabilize Protein Structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-04-29 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9795 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.948, 100.036, 125.218 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.890 - 1.850 |
R-factor | 0.1718 |
Rwork | 0.169 |
R-free | 0.21830 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2h2w |
RMSD bond length | 0.017 |
RMSD bond angle | 2.006 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 78.157 | 29.876 | 1.950 |
High resolution limit [Å] | 1.850 | 5.850 | 1.850 |
Rmerge | 0.058 | 1.523 | |
Rmeas | 0.162 | 0.061 | 1.581 |
Rpim | 0.044 | 0.017 | 0.419 |
Number of reflections | 56066 | 1932 | 8044 |
<I/σ(I)> | 11.5 | 1.8 | |
Completeness [%] | 99.3 | 97.9 | 99.3 |
Redundancy | 13.4 | 11.9 | 13.9 |
CC(1/2) | 0.998 | 0.721 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 277 | 100mM Potassium Formate and 26% PEG 3350 |