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 |