2VPI
Human GMP synthetase - glutaminase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.680, 120.880, 47.320 |
| Unit cell angles | 90.00, 106.43, 90.00 |
Refinement procedure
| Resolution | 19.770 - 2.400 |
| R-factor | 0.206 |
| Rwork | 0.203 |
| R-free | 0.26100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gpm |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.227 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0040) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.140 | 0.560 |
| Number of reflections | 14466 | |
| <I/σ(I)> | 11.52 | 2.96 |
| Completeness [%] | 96.0 | 92.4 |
| Redundancy | 4.13 | 3.88 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 0.2 M AMMONIUM ACETATE 0.1 M BIS-TRIS PH 5.5 25% PEG 3350 |
