2JH3
The crystal structure of DR2241 from Deinococcus radiodurans at 1.9 A resolution reveals a multi-domain protein with structural similarity to chelatases but also with two additional novel domains
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 124.780, 128.690, 135.080 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.19 |
| Rwork | 0.189 |
| R-free | 0.23800 |
| Structure solution method | SIRAS |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.841 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.080 | 0.620 |
| Number of reflections | 168727 | |
| <I/σ(I)> | 9.3 | 1.9 |
| Completeness [%] | 98.8 | 98.6 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.8 | 17-20% PEG3350 AND 0.15-0.20 M MGCL2., pH 8.80 |
