7LXF
ENAH EVH1 domain bound to peptide from protein PCARE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-07-11 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.979180 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 52.120, 52.120, 197.850 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.140 - 1.650 |
R-factor | 0.2182 |
Rwork | 0.217 |
R-free | 0.23450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6rd2 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.140 | 45.140 | 1.690 |
High resolution limit [Å] | 1.650 | 7.380 | 1.650 |
Rmerge | 0.066 | 0.034 | 4.117 |
Rmeas | 0.067 | 0.035 | 4.199 |
Total number of observations | 742720 | ||
Number of reflections | 20302 | 320 | 1449 |
<I/σ(I)> | 26.94 | 94.78 | 0.79 |
Completeness [%] | 99.9 | 99.1 | 99.3 |
Redundancy | 36.584 | 28.366 | 25.983 |
CC(1/2) | 1.000 | 1.000 | 0.702 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.1M Tris pH 8.0, 3.30M NaCl |