1MGY
Structure of the D85S mutant of bacteriorhodopsin with bromide bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-01-07 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.1272 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 52.498, 121.326, 73.875 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 2.000 |
Rwork | 0.215 |
R-free | 0.23650 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kgb |
RMSD bond length | 0.007 |
RMSD bond angle | 0.953 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.127 * | 0.350 * |
Total number of observations | 135550 * | |
Number of reflections | 16336 | |
Completeness [%] | 94.2 | 89.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 4.6 | 293 | Sodium Acetate, PEG 4000, potassium chloride, mono-olein, pH 4.6, connected bilayer gel, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 15 (mg/ml) | |
2 | 1 | 2 | sodium acetate | 100 (mM) | pH4.6 |
3 | 1 | 2 | 200 (mM) | ||
4 | 1 | 2 | PEG4000 | 10 (%) |