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 |