2ZXG
Aminopeptidase N complexed with the aminophosphinic inhibitor of PL250, a transition state analogue
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 | 2007-01-25 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 120.700, 120.700, 171.000 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.550 |
| R-factor | 0.17895 |
| Rwork | 0.178 |
| R-free | 0.19477 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 2dq6 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.202 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.650 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.089 | 0.288 |
| Number of reflections | 207284 | |
| <I/σ(I)> | 35.7 | 7.9 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 6.7 | 7.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 298 | 1.75M ammonium sulfate, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
