6UEL
CPS1 bound to allosteric inhibitor H3B-193
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 120 |
Detector technology | PIXEL |
Collection date | 2019-06-20 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 99.587, 132.342, 142.443 |
Unit cell angles | 90.00, 102.57, 90.00 |
Refinement procedure
Resolution | 139.030 - 1.900 |
R-factor | 0.1739 |
Rwork | 0.172 |
R-free | 0.20860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5dot |
RMSD bond length | 0.019 |
RMSD bond angle | 1.841 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 139.030 | 50.000 | 1.930 |
High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
Rmerge | 0.098 | 0.050 | 0.987 |
Rmeas | 0.110 | 0.055 | 1.110 |
Rpim | 0.048 | 0.024 | 0.499 |
Number of reflections | 281085 | 14056 | 14009 |
<I/σ(I)> | 6.2 | ||
Completeness [%] | 99.3 | 97.5 | 99.7 |
Redundancy | 5 | 5.1 | 4.8 |
CC(1/2) | 0.993 | 0.611 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | CPS1 protein was buffer exchanged into 50 mM glycyl-glycine pH 7.4, 50 mM KCl, 5% glycerol. CPS1 was concentrated to 10 mg/ml and H3B-4193 was added to a 5x excess molar ratio along with 1mM AMPPNP and 1mM NAG. Ligand bound complex crystals grew by hanging drop vapor diffusion in 20% PEG 3350 and 0.2M trisodium citrate |