3W6X
Yeast N-acetyltransferase Mpr1 in complex with CHOP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-01 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.98508 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 80.345, 229.340, 84.755 |
| Unit cell angles | 90.00, 90.94, 90.00 |
Refinement procedure
| Resolution | 56.945 - 2.299 |
| R-factor | 0.1683 |
| Rwork | 0.166 |
| R-free | 0.21450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3w91 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.361 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHENIX ((autosol)) |
| Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.945 | 2.420 |
| High resolution limit [Å] | 2.299 | 2.300 |
| Rmerge | 0.098 | 0.453 |
| Number of reflections | 134196 | |
| <I/σ(I)> | 8 | 2.5 |
| Completeness [%] | 100.0 | 98.9 |
| Redundancy | 3.8 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 23%(w/v) PEG 3350, 0.1M bis-tris, 0.2M MgCl2, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
