4MO9
Crystal Structure of TroA-like Periplasmic Binding Protein FepB from Veillonella parvula
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-04-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97987 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.402, 75.999, 125.187 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.361 - 1.925 |
R-factor | 0.168 |
Rwork | 0.166 |
R-free | 0.19900 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.035 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | PHENIX ((phenix.refine: dev_1367)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.960 |
High resolution limit [Å] | 1.930 | 1.930 |
Number of reflections | 29285 | |
<I/σ(I)> | 9.9 | 2 |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.8 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.2 M Trimethylamine N-oxide, 0.1 M Tris pH 8.5, 20 %(w/v) PEGMME2000, VAPOR DIFFUSION, SITTING DROP, temperature 289K |