1RHZ
The structure of a protein conducting channel
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-03-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9799 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 92.746, 149.361, 79.475 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 9.990 - 3.500 |
R-factor | 0.254 |
Rwork | 0.254 |
R-free | 0.33400 * |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 19.600 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 3.700 |
High resolution limit [Å] | 3.500 | 3.500 |
Rmerge | 0.080 * | 0.670 * |
Number of reflections | 14439 * | 1291 * |
<I/σ(I)> | 30.9 | 2.74 |
Completeness [%] | 98.4 * | 89.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 4 * | Peg 400, Glycine buffer, glycerol, sodium chloride, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-10 (mg/ml) | |
2 | 1 | reservoir | PEG400 | 50-55 (%) | |
3 | 1 | reservoir | glycine | 50 (mM) | pH9.0-9.5 |