3IWW
Crystal structure of human glutamate carboxypeptidase II (GCPII) in a complex with DBIBzL, a urea-based inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 101.068, 130.035, 157.951 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.16621 |
| Rwork | 0.165 |
| R-free | 0.20581 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2oot |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.822 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.125 | 0.447 |
| Number of reflections | 56427 | |
| <I/σ(I)> | 16 | 3.2 |
| Completeness [%] | 99.8 | 98.5 |
| Redundancy | 5.6 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 33% v/v pentaerythritol propoxylate PO/OH 5/4, 1.5 % w/v PEG 3350, 100 mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
