4MCQ
A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyldi-gamma-L-glutamic acid (pteroyltri-gamma-L-glutamic acid)
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 |
| Collection date | 2010-03-03 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.918 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 101.646, 130.140, 159.867 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.960 - 2.000 |
| R-factor | 0.13797 |
| Rwork | 0.137 |
| R-free | 0.17168 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.664 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.051 | 0.226 |
| Number of reflections | 72031 | |
| <I/σ(I)> | 30.1 | 5 |
| Completeness [%] | 99.3 | 94.8 |
| Redundancy | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 33% (v/v) pentaerythritol, propoxylate PO/OH 5/4, 0.5% (w/v) PEG 3350, 0.10 M Tris HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
