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 |