7WAB
Crystal structure of the prolyl endoprotease, PEP, from Aspergillus niger
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-1A |
Synchrotron site | Photon Factory |
Beamline | BL-1A |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2010-06-22 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.97 |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 144.517, 144.517, 56.542 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 17.140 - 1.750 |
R-factor | 0.1654 |
Rwork | 0.164 |
R-free | 0.19310 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.17) |
Phasing software | MOLREP |
Refinement software | PHENIX (1.19) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 44.530 | 44.530 | 1.780 |
High resolution limit [Å] | 1.750 | 9.090 | 1.750 |
Rmerge | 0.061 | 0.034 | 0.422 |
Rmeas | 0.066 | 0.037 | 0.490 |
Rpim | 0.022 | 0.012 | 0.245 |
Total number of observations | 3224 | 8981 | |
Number of reflections | 107457 | 441 | 2491 |
<I/σ(I)> | 17.5 | 32.4 | 1.8 |
Completeness [%] | 93.2 | 88.2 | 75.6 |
Redundancy | 7.2 | 7.3 | 3.6 |
CC(1/2) | 0.998 | 0.999 | 0.810 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 2.5 | 293 | 0.1M glycine buffer pH 2.5, 2.72M NaCl, 3% isopropanol |