1P3E
Structure of Glu endopeptidase in complex with MPD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-01 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.10 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 61.936, 55.757, 60.195 |
| Unit cell angles | 90.00, 118.17, 90.00 |
Refinement procedure
| Resolution | 19.690 - 1.720 |
| R-factor | 0.16791 |
| Rwork | 0.166 |
| R-free | 0.20809 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1p3c |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.420 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.760 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Number of reflections | 18778 | |
| Completeness [%] | 93.0 | 95.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 0.01 M Tris-HCl buffer, pH 7.0, 2 mM CaCl2, 1.2 M potassium phosphate, 3% MPD, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
