3A54
Crystal structure of the A47Q1 mutant of pro-protein-glutaminase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-06 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.986, 104.113, 134.189 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.894 - 1.502 |
| R-factor | 0.1412 |
| Rwork | 0.140 |
| R-free | 0.16740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3a56 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.020 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.037 | 0.402 |
| Number of reflections | 125864 | |
| <I/σ(I)> | 17.5 | 2.7 |
| Completeness [%] | 98.6 | 91.5 |
| Redundancy | 4.3 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 293 | 20% PEG 3350, 0.2M ammonium tartrate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
