3GSD
2.05 Angstrom structure of a divalent-cation tolerance protein (CutA) from Yersinia pestis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-27 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 140.782, 157.914, 157.132 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.590 - 2.050 |
| R-factor | 0.15868 |
| Rwork | 0.156 |
| R-free | 0.20039 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nuh |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.209 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.590 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.506 | |
| Number of reflections | 107769 | |
| <I/σ(I)> | 17.7 | 3.3 |
| Completeness [%] | 98.1 | 94.8 |
| Redundancy | 5.9 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | Protein solution: 0.3M NaCl, 10mM HEPES pH 7.5. Well solution: 20% PEG 3350, 0.2M Sodium citrate, 0.1M HEPES pH 7.5. Cryo solution: 7% Glycerol, 7% Sucrose, 7% Ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
