3A56
Crystal structure 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 | 2008-07-06 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.644, 103.290, 132.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.551 - 1.728 |
| R-factor | 0.1762 |
| Rwork | 0.175 |
| R-free | 0.20610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zk9 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.067 |
| 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] | 50.000 | 1.790 |
| High resolution limit [Å] | 1.728 | 1.730 |
| Rmerge | 0.056 | 0.314 |
| Number of reflections | 80701 | |
| Completeness [%] | 98.2 | 90.9 |
| Redundancy | 6.6 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.1 | 293 | 0.2M Ammonium Citrate dibasic, 20% PEG 3350, pH 5.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
