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 |