4HXG
Pyrococcus horikoshii acylaminoacyl peptidase (orthorhombic crystal form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-29 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0715 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 183.310, 183.800, 275.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.980 - 2.700 |
| R-factor | 0.2002 |
| Rwork | 0.200 |
| R-free | 0.24070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hxf |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.979 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.720 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.090 | 0.690 |
| Number of reflections | 255208 | |
| <I/σ(I)> | 16.47 | 2.36 |
| Completeness [%] | 94.9 | 96.8 |
| Redundancy | 4.39 | 4.335 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
