5HL6
Crystal Structure of a Putative GAF sensor protein from Burkholderia vietnamiensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 44.460, 70.200, 103.070 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.819 - 1.850 |
| R-factor | 0.173 |
| Rwork | 0.171 |
| R-free | 0.21350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ksf |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.711 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MoRDa |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.900 | |
| High resolution limit [Å] | 1.849 | 8.270 | 1.849 |
| Rmerge | 0.058 | 0.022 | 0.604 |
| Rmeas | 0.063 | 0.024 | 0.664 |
| Total number of observations | 164660 | ||
| Number of reflections | 28101 | 344 | 2028 |
| <I/σ(I)> | 19.82 | 52.53 | 3.23 |
| Completeness [%] | 99.4 | 90.8 | 100 |
| Redundancy | 5.8 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 290 | BuviA.00048.a.B1.PS02344 at 57.5 mg/ml was mixed 1:1 with JCSG+(c1): 20% PEG-8000, 100 mM sodium phosphate dibasic/ citric acid, pH = 4.2, 200 mM NaCl, and cryoprotected with 20% ethylene glycol |






