2XTU
Structure of E.coli rhomboid protease GlpG active site mutant, S201T in trigonal 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 | 2009-02-20 |
Detector | ADSC CCD |
Spacegroup name | H 3 2 |
Unit cell lengths | 110.250, 110.250, 127.600 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.223 - 1.850 |
R-factor | 0.1773 |
Rwork | 0.176 |
R-free | 0.19820 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3b45 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.982 |
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] | 42.530 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.090 | 0.570 |
Number of reflections | 25582 | |
<I/σ(I)> | 12.2 | 2.8 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 5.3 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 2.5M AMMONIUM CHLORIDE, 0.1M BIS-TRIS PH7.0, 298K |