2Y2D
crystal structure of AmpD holoenzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-14 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 32 |
| Unit cell lengths | 67.691, 67.691, 92.805 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 9.997 - 2.000 |
| R-factor | 0.2108 |
| Rwork | 0.205 |
| R-free | 0.27830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2y28 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.195 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.800 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.110 | 0.480 |
| Number of reflections | 32155 | |
| <I/σ(I)> | 23 | 5.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.4 | 11.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 0.1 M TRIS PH 6.0, 0.1 M LI2SO4, 28% PEG 3350 |
