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 |