5FEA
Domain Swapped Bromodomain from Leishmania donovani
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97921 |
| Spacegroup name | P 64 2 2 |
| Unit cell lengths | 77.176, 77.176, 169.496 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.600 |
| R-factor | 0.23 |
| Rwork | 0.228 |
| R-free | 0.27720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5c8g |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.136 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.640 |
| High resolution limit [Å] | 2.600 | 7.050 | 2.600 |
| Rmerge | 0.099 | 0.052 | 0.698 |
| Rmeas | 0.102 | 0.054 | 0.718 |
| Rpim | 0.025 | 0.014 | 0.165 |
| Total number of observations | 173005 | ||
| Number of reflections | 9764 | ||
| <I/σ(I)> | 10.1 | ||
| Completeness [%] | 98.9 | 96.8 | 98.5 |
| Redundancy | 17.7 | 15 | 18.7 |
| CC(1/2) | 0.998 | 0.984 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | The protein (concentrated to 15mg/mL in 20mM HEPES pH 7.5 and 150 mM NaCl) was crystallized at 293 K in 30% PEG2000 MME, 0.15M KBr with bromosporine using the sitting drop method. |
