1F47
THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-12-12 |
Detector | RIGAKU RAXIS |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 36.526, 38.901, 54.541 |
Unit cell angles | 90.00, 104.11, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.950 |
R-factor | 0.205 |
Rwork | 0.205 |
R-free | 0.25100 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.420 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.055 | 0.146 |
Number of reflections | 10556 | |
<I/σ(I)> | 26.9 | |
Completeness [%] | 95.6 | 88.6 |
Redundancy | 3.92 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 * | 291 | 30% PEG 6000, 100 mM Bicine, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 25 (%) | |
3 | 1 | reservoir | MES | 100 (mM) |