7LL9
D-Protein RFX-V2 Bound to the VEGFR1 Domain 3 Site on VEGF-A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-09-15 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.1158 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 66.850, 120.437, 120.437 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 58.520 - 2.900 |
R-factor | 0.2651 |
Rwork | 0.263 |
R-free | 0.31530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3qtk |
RMSD bond length | 0.010 |
RMSD bond angle | 1.795 |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.3) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 120.440 | 120.440 | 3.080 |
High resolution limit [Å] | 2.900 | 8.700 | 2.900 |
Rmerge | 0.061 | 0.025 | 1.100 |
Rmeas | 0.064 | 0.026 | 1.147 |
Rpim | 0.018 | 0.008 | 0.320 |
Total number of observations | 285459 | 9778 | 44567 |
Number of reflections | 22242 | 925 | 3523 |
<I/σ(I)> | 25.7 | 70.7 | 2.4 |
Completeness [%] | 99.9 | 99.1 | 99.9 |
Redundancy | 12.8 | 10.6 | 12.7 |
CC(1/2) | 1.000 | 1.000 | 0.775 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291.2 | magnesium chloride, Bis-Tris, PEG3350 |