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 |