4C1M
Myeloperoxidase in complex with the revesible inhibitor HX1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-11-28 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 111.279, 63.440, 92.381 |
| Unit cell angles | 90.00, 97.36, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.22521 |
| Rwork | 0.222 |
| R-free | 0.27754 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cxp |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.142 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.090 | 0.270 |
| Number of reflections | 81456 | |
| <I/σ(I)> | 6.2 | 2.6 |
| Completeness [%] | 94.4 | 93.8 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
