5B51
Crystal structure of heme binding protein HmuT R242A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-06-29 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.90 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 73.060, 73.060, 147.070 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.270 - 1.300 |
| R-factor | 0.16343 |
| Rwork | 0.163 |
| R-free | 0.18066 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5az3 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.351 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.680 | 1.340 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.069 | 0.487 |
| Number of reflections | 96893 | |
| <I/σ(I)> | 17.52 | 4.58 |
| Completeness [%] | 98.3 | 98.3 |
| Redundancy | 9.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 1.90 M Ammonium sulfate, 0.19 M Ammonium tartrate, 0.16 M Potassium thiocyanate |
