1II0
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 | 2000-02-21 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 76.727, 222.189, 74.126 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.610 - 2.400 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.25200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.600 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 28.600 |
High resolution limit [Å] | 2.400 |
Rmerge | 0.076 |
Total number of observations | 316955 * |
Number of reflections | 46952 * |
<I/σ(I)> | 16.9 |
Completeness [%] | 90.0 |
Redundancy | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 30 * | PEG3000, ATP, MgCl2, NaAsO2, CdCl2, Bistrispropane, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 303K |
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)) | |
8 | 1 | reservoir | Bis-Tris propane | 100 (mM) |