2FXA
Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-06-05 |
| Detector | CUSTOM-MADE |
| Wavelength(s) | 0.97887, 0.97943 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.272, 79.909, 131.239 |
| Unit cell angles | 90.00, 100.18, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.400 |
| R-factor | 0.20945 |
| Rwork | 0.208 |
| R-free | 0.23392 |
| Structure solution method | MAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.500 |
| Data reduction software | d*TREK |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 41448 | |
| Completeness [%] | 99.4 | 91.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 292 | 0.2M K/Na tartrate tetrahydrate, 20% PEG 3350, pH 7.5, VAPOR DIFFUSION, temperature 292K |
