1NZA
Divalent cation tolerance protein (Cut A1) from thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-01-27 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 83.003, 83.003, 83.003 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.700 |
| Rwork | 0.229 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kr4 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (1.1) |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.073 | 0.479 |
| Number of reflections | 230757 | |
| <I/σ(I)> | 51.26 | 7.9 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 21.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 6.6 | 295 | NA ACETATE 1.65M, MES 0.1M , pH 6.6, MICROBATCH, temperature 295K |






