1F48
CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-08-30 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 73.523, 75.715, 222.714 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.370 - 2.300 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| R-free | 0.26300 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.800 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.086 | 0.651 |
| Total number of observations | 178456 * | |
| Number of reflections | 27783 | |
| <I/σ(I)> | 18.8 | |
| Completeness [%] | 98.2 | 91.4 |
| Redundancy | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 303 | Zhou, T., (1999) Acta Crystallogr., D55, 921. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | ADP | 2 (mM) | |
| 3 | 1 | drop | 1 (mM) | ||
| 4 | 1 | drop | 2 (mM) | ||
| 5 | 1 | drop | 1 (mM) | ||
| 6 | 1 | drop | Bis-Tris propane | 10 (mM) | |
| 7 | 1 | reservoir | PEG3000 | 4 (%(w/v)) |
