4E98
Crystal structure of possible CutA1 divalent ion tolerance protein from Cryptosporidium parvum Iowa II
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-02-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 94.460, 55.590, 67.290 |
| Unit cell angles | 90.00, 108.21, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.2 |
| Rwork | 0.198 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nza |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.568 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.093 | 0.472 |
| Number of reflections | 22553 | |
| <I/σ(I)> | 13.3 | 3.58 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 5.5 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 290 | Emerald Bio Precipitant Synergy Screen: 30% PEG1500, 20% PEG400, 100 mM HEPES, pH 7.5, CRPAA.01087.AA1 PB00061 at 3 mg/mL, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
