5X1Y
Structure of mercuric reductase from Lysinibacillus sphaericus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-30 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 236.380, 150.270, 122.780 |
| Unit cell angles | 90.00, 92.62, 90.00 |
Refinement procedure
| Resolution | 87.072 - 3.480 |
| R-factor | 0.1937 |
| Rwork | 0.191 |
| R-free | 0.23960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zk7 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.619 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 87.072 |
| High resolution limit [Å] | 3.480 |
| Number of reflections | 55103 |
| <I/σ(I)> | 18.93 |
| Completeness [%] | 100.0 |
| Redundancy | 11 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 7 | 289 | 5% v/v Tascimate, 0.1 M HEPES, pH 7.0 and 10% w/v PEG monomethyl ether 5000 |
