1B0U
ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-06-15 |
Detector | ADSC |
Wavelength(s) | 1.000, 0.9800, 0.97977, 0.9686 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 68.809, 68.809, 148.033 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.21100 |
Structure solution method | MAD |
RMSD bond length | 0.018 |
RMSD bond angle | 23.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (0.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.050 | 0.266 |
Number of reflections | 56098 | |
<I/σ(I)> | 10.4 | 3.8 |
Completeness [%] | 97.0 | 88.1 |
Redundancy | 3.7 | 2.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | sparse matrix method * | 7 | pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 15 (mg/ml) | |
10 | 1 | 2 | ATP | 10 (mM) | |
2 | 1 | 1 | glycerol | 20 (%) | |
3 | 1 | 1 | EDTA | 2 (mM) | |
4 | 1 | 1 | imidazol | 50 (mM) | |
5 | 1 | 1 | HEPES | 0.1 (M) | |
6 | 1 | 1 | ATP | 10 (mM) | |
7 | 1 | 2 | PEG6000 | 20 (%) | |
8 | 1 | 2 | 1.2 (M) | ||
9 | 1 | 2 | HEPES | 0.1 (M) |