2HPG
The crystal structure of a thermophilic TRAP periplasmic binding protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97167, 0.97934, 0.97920 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 119.260, 119.260, 429.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.215 |
| Rwork | 0.213 |
| R-free | 0.23900 |
| Structure solution method | MAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.249 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | SHELXS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 103.282 | 30.010 | 2.000 |
| High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
| Rmerge | 0.094 | 0.039 | 0.405 |
| Total number of observations | 47653 | 171983 | |
| Number of reflections | 142555 | ||
| <I/σ(I)> | 6.2 | 13.9 | 1.9 |
| Completeness [%] | 100.0 | 99.2 | 100 |
| Redundancy | 9.6 | 9.5 | 8.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | 290 | 0.1M Phosphate/Citrate pH4.2, 2.5M Ammonium Sulfate , VAPOR DIFFUSION, HANGING DROP, temperature 290K |
