3N00
Crystal Structure of a deletion mutant of human Reverba ligand binding domain bound with an NCoR ID1 peptide determined to 2.60A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 112.550, 112.550, 103.833 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.040 - 2.600 |
| R-factor | 0.20035 |
| Rwork | 0.199 |
| R-free | 0.26633 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1db1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.126 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (6.0.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.049 | 0.296 |
| Number of reflections | 7921 | |
| <I/σ(I)> | 50.5 | 7.3 |
| Completeness [%] | 99.9 | 99.4 |
| Redundancy | 10.9 | 9.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 295 | 1ul of precipitant composed of 6-9% of PEG 3350, 8% glycerol, 200mM proline, 80mM HEPES was mixed with 1uL of the Rev-erba NCoR complex at 5-6 mG/Lit to obtain diffraction grade crystals, pH 7.5, VAPOR DIFFUSION, temperature 295K |
