8HKR
Crystal Structure of Histone H3 Lysine 79 (H3K79) Methyltransferase Rv2067c from Mycobacterium tuberculosis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-12-02 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.699996 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 109.150, 109.150, 216.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.810 - 2.400 |
R-factor | 0.2025 |
Rwork | 0.202 |
R-free | 0.21830 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Determined using iodine SAD; experimental phasing |
RMSD bond length | 0.005 |
RMSD bond angle | 1.337 |
Data reduction software | XDS (1.12) |
Data scaling software | XSCALE (Jan 10, 2022 BUILT=20220820) |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.810 | 48.810 | 2.460 |
High resolution limit [Å] | 2.400 | 10.730 | 2.400 |
Rmerge | 0.089 | 0.038 | 2.223 |
Rmeas | 0.090 | 0.039 | 2.268 |
Total number of observations | 1319560 | ||
Number of reflections | 51986 | 688 | 3783 |
<I/σ(I)> | 24.37 | 70.47 | 1.71 |
Completeness [%] | 100.0 | 98.6 | 100 |
Redundancy | 25.383 | 22.384 | 25.633 |
CC(1/2) | 0.999 | 0.999 | 0.741 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | Buffer: 0.1 M imidazole/MES acid, pH 6.5: Precipitant: 20% w/v polyethylene glycol 500* monomethyl ether + 10% w/v polyethylene glycol 20,000: Additive: 0.03 M sodium nitrate + 0.03 M sodium phosphate dibasic + 0.03 M ammonium sulfate |