2Q2H
Crystal structure of the protein secretion chaperone CsaA from Agrobacterium tumefaciens with a genetically fused phage-display derived peptide substrate at the N-terminus.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-10-27 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 61 |
| Unit cell lengths | 60.528, 60.528, 115.247 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 23.860 - 1.650 |
| R-factor | 0.161 |
| Rwork | 0.160 |
| R-free | 0.17300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gd7 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.183 |
| 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] | 23.860 | 1.710 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.039 | 0.162 |
| Total number of observations | 6400 | |
| Number of reflections | 25681 | |
| <I/σ(I)> | 30 | 8.6 |
| Completeness [%] | 89.4 | 49.7 |
| Redundancy | 5.71 | 4.47 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 292 | 30% PEG 4000, 0.4 M ammonium acetate, 0.1 M sodium citrate pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
