4NGM
Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.91841 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 101.300, 130.193, 158.789 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.030 - 1.840 |
| R-factor | 0.1714 |
| Rwork | 0.170 |
| R-free | 0.20570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.969 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 49.032 | 1.950 | |
| High resolution limit [Å] | 1.840 | 5.490 | 1.840 |
| Rmerge | 0.068 | 0.022 | 0.467 |
| Rmeas | 0.027 | 0.591 | |
| Number of reflections | 90745 | 6437 | 28172 |
| <I/σ(I)> | 11.31 | 37.26 | 1.91 |
| Completeness [%] | 99.0 | 96.7 | 98.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop | 8 | 289 | Tris-HCl, PEG 3350, pentaerythritol propoxylate, pH 8.0, hanging drop, temperature 289K |
