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 |