3CUS
Structure of a double ILE/PHE mutant of NI-FE hydrogenase refined at 2.2 angstrom resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-01-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.400, 99.960, 182.690 |
| Unit cell angles | 90.00, 92.23, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.18677 |
| Rwork | 0.185 |
| R-free | 0.22223 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yqw |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.266 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.300 |
| High resolution limit [Å] | 2.180 | 2.180 |
| Rmerge | 0.070 | 0.198 |
| Number of reflections | 108157 | |
| <I/σ(I)> | 7.2 | 3.3 |
| Completeness [%] | 93.3 | 71 |
| Redundancy | 2.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | PEG6000, GLYCEROL, PH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
