5TEU
Brucella periplasmic binding protein YehZ
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-07-02 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9787 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 111.370, 111.370, 122.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.120 - 1.620 |
| R-factor | 0.1599 |
| Rwork | 0.159 |
| R-free | 0.18490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ne4 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.085 |
| Data reduction software | xia2 (-3da) |
| Data scaling software | xia2 (-3da) |
| Phasing software | PHENIX (1.9_1692) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.120 | 1.660 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Rmerge | 0.061 | 0.857 |
| Number of reflections | 97517 | |
| <I/σ(I)> | 26.6 | 3.4 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 12.2 | 12.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 292.15 | 200 mM K/Na tartrate, 2.2 M Ammonium Sulfate |
