2Q2I
Crystal structure of the protein secretion chaperone CsaA from Agrobacterium tumefaciens.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-08-24 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 61 |
| Unit cell lengths | 60.653, 60.653, 113.389 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 52.530 - 1.550 |
| R-factor | 0.18 |
| Rwork | 0.178 |
| R-free | 0.20800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gd7 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.282 |
| Data reduction software | CrystalClear |
| Data scaling software | d*TREK (8.0SSI) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.530 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.040 | 0.341 |
| Total number of observations | 35222 | |
| Number of reflections | 34123 | |
| <I/σ(I)> | 23.7 | 7.2 |
| Completeness [%] | 99.8 | 99.6 |
| Redundancy | 10.82 | 10.13 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 1.8M ammonium sulfate, 0.1M HEPES pH 7.5, 2% PEG400, 5% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 294K |






