5X49
Crystal Structure of Human mitochondrial X-prolyl Aminopeptidase (XPNPEP3)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
Synchrotron site | RRCAT INDUS-2 |
Beamline | PX-BL21 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-07-29 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97947 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.897, 135.103, 67.205 |
Unit cell angles | 90.00, 99.87, 90.00 |
Refinement procedure
Resolution | 30.983 - 1.650 |
R-factor | 0.1552 |
Rwork | 0.154 |
R-free | 0.17750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wl9 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.069 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2152)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.280 | 1.680 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.062 | 0.636 |
Number of reflections | 130822 | |
<I/σ(I)> | 12.9 | 2.2 |
Completeness [%] | 98.8 | 99.8 |
Redundancy | 3.7 | 3.7 |
CC(1/2) | 0.998 | 0.742 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 294 | 10 mM TrisCl, 100 mM NaCl, 50 mM HEPES, 10% PEG 3350, 2.5 mM Apstatin |