2XTV
Structure of E.coli rhomboid protease GlpG, active site mutant, S201T, orthorhombic crystal form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-29 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.630, 58.870, 91.090 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.009 - 1.700 |
| R-factor | 0.1877 |
| Rwork | 0.186 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xov |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.041 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.540 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.050 | 0.310 |
| Number of reflections | 22469 | |
| <I/σ(I)> | 13.3 | 3.2 |
| Completeness [%] | 95.8 | 86.9 |
| Redundancy | 3.3 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 1.5M NACL, 0.1M BIS-TRIS, PH7, 2% DMPC/CHAPSO, (ADDED ONLY TO THE PROTEIN), 298K, pH 7.0 |
