7MSB
Structure of EED bound to EEDi-4259
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-10-04 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 57.867, 85.024, 91.988 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.000 - 1.900 |
| R-factor | 0.162 |
| Rwork | 0.160 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | in house structure |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.030 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Rmerge | 0.093 | 0.027 | 0.661 |
| Rmeas | 0.101 | 0.029 | 0.711 |
| Rpim | 0.037 | 0.011 | 0.262 |
| Total number of observations | 269118 | ||
| Number of reflections | 36678 | 2000 | 1799 |
| <I/σ(I)> | 7.3 | ||
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 7.3 | 6.7 | 7.3 |
| CC(1/2) | 0.999 | 0.855 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 2uL of protein + 2 uL of well (0.1 M Tris pH 8.5, 20% glycerol, 4.3 M Na Formate, 10 mM TCEP) |
