3Q1C
Structure of EspG Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-16 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.150, 74.378, 93.921 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.093 - 1.596 |
R-factor | 0.1622 |
Rwork | 0.161 |
R-free | 0.18810 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.967 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 32.958 | 50.000 | 1.660 |
High resolution limit [Å] | 1.595 | 3.450 | 1.600 |
Rmerge | 0.035 | ||
Number of reflections | 60098 | ||
<I/σ(I)> | 32 | ||
Redundancy | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 2.0-11.0% PEG8000, 100 mM Bis-Tris, pH 6.25-7.5, VAPOR DIFFUSION, HANGING DROP, temperature range 268-291K |