2NRF
Crystal Structure of GlpG, a Rhomboid family intramembrane protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-09-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793 |
Spacegroup name | P 31 |
Unit cell lengths | 59.458, 59.458, 118.048 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 100.000 - 2.600 |
R-factor | 0.285 |
Rwork | 0.262 |
R-free | 0.29500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ic8 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.837 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.071 | 0.508 |
Number of reflections | 14184 | |
<I/σ(I)> | 15.1 | |
Completeness [%] | 98.5 | 93.9 |
Redundancy | 9 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 295 | PEG 3000 7%, Li2S04 100 mM, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K |