4FT2
crystal structure of Zea mays ZMET2 in complex H3(1-15)K9me2 peptide and SAH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-14 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 |
| Unit cell lengths | 64.861, 88.858, 113.501 |
| Unit cell angles | 93.15, 95.72, 110.70 |
Refinement procedure
| Resolution | 40.099 - 3.200 |
| R-factor | 0.2373 |
| Rwork | 0.235 |
| R-free | 0.27730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fsx |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.575 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.118 | 0.503 |
| Number of reflections | 38805 | |
| <I/σ(I)> | 12.6 | 2.2 |
| Completeness [%] | 99.0 | 98.8 |
| Redundancy | 3.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | 0.2 M calcium acetate, 0.1 M imidazole pH 8.0, and 10% PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
