2VQA
Protein-folding location can regulate Mn versus Cu- or Zn-binding. Crystal Structure of MncA.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 236.190, 236.190, 134.041 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 58.320 - 2.950 |
| R-factor | 0.193 |
| Rwork | 0.191 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l3j |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.308 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.200 | 3.110 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.180 | 0.430 |
| Number of reflections | 46724 | |
| <I/σ(I)> | 13.4 | 5.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.9 | 11.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.2 | 0.1M SODIUM ACETATE PH 3.25, 8% W/V PEG8000 |
