7KAE
Rop protein variant with a buried tryptophan
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2019-03-07 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9790 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.881, 40.016, 72.271 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 1.600 |
R-factor | 0.1956 |
Rwork | 0.194 |
R-free | 0.22360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rop |
RMSD bond length | 0.014 |
RMSD bond angle | 1.936 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.140 | 1.630 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.041 | |
Rmeas | 0.044 | 0.243 |
Rpim | 0.016 | |
Number of reflections | 14720 | 690 |
<I/σ(I)> | 14.7 | |
Completeness [%] | 96.8 | |
Redundancy | 7.3 | |
CC(1/2) | 0.999 | 0.970 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 295 | 28% (w/v) PEG 400, 300 mM NaCl, 100 mM NaHEPES |