8B57
Structure of prolyl endoprotease from Aspergillus niger CBS 109712
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 | 2009-02-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9195 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 162.030, 162.030, 162.030 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.240 - 2.420 |
| R-factor | 0.17151 |
| Rwork | 0.170 |
| R-free | 0.20892 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | composite model |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.403 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | MR-Rosetta |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.240 | 2.550 |
| High resolution limit [Å] | 2.420 | 2.420 |
| Rmerge | 0.108 | 0.636 |
| Number of reflections | 27027 | 3897 |
| <I/σ(I)> | 14.5 | 3.7 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 9.2 | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 26-29% (w/v) PEG 3350, 0.1 M sodium citrate pH 5.0, 0.1 M ammonium tartrate pH 7.2, 20 mM HAc/NaAc pH 5.0, 50 mM NaCl |
