3FEC
Crystal structure of human Glutamate Carboxypeptidase III (GCPIII/NAALADase II), pseudo-unliganded
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 122.767, 104.322, 78.008 |
| Unit cell angles | 90.00, 107.69, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.490 |
| R-factor | 0.15902 |
| Rwork | 0.159 |
| R-free | 0.18320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2or4 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.884 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.4.0057) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.540 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.079 | 0.525 |
| Number of reflections | 148978 | |
| <I/σ(I)> | 2 | |
| Completeness [%] | 98.7 | 93.6 |
| Redundancy | 4.9 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.1 M HEPES-Na, 10% (w/v) PEG6000, 5% (v/v) MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
