4PK1
Structure of BamB fused to a BamA POTRA domain fragment
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-08-06 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.270, 91.410, 61.210 |
Unit cell angles | 90.00, 92.85, 90.00 |
Refinement procedure
Resolution | 19.890 - 3.100 |
Rwork | 0.251 |
R-free | 0.28100 |
Structure solution method | MOLECULAR REPLACEMENT |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.900 | 3.150 |
High resolution limit [Å] | 3.100 | 3.100 |
Number of reflections | 9870 | |
<I/σ(I)> | 11 | 1.9 |
Completeness [%] | 99.9 | 100 |
Redundancy | 3.7 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289 | The BamA-BamB chimera protein was crystallized at 16 degC by sitting drop vapor diffusion method. Initial crystallizing conditions were refined in a hanging drop in the following solution: 1.4M Ammonium sulfate, 9% 2-propanol, and 0.1M Sodium acetate pH 5.5. We used 1.5 uL of the 20mg/ml protein mixed with 1.5 uL mother liquor in a reservoir filled with 500 uL precipitant solution |