1MKZ
Crystal structure of MoaB protein at 1.6 A resolution.
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | CUSTOM-MADE |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 69.169, 69.169, 126.184 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 129.100 - 1.600 |
R-factor | 0.18461 |
Rwork | 0.183 |
R-free | 0.21900 * |
RMSD bond length | 0.020 |
RMSD bond angle | 1.885 |
Data reduction software | HKL-2000 |
Data scaling software | d*TREK |
Phasing software | CNS |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 129.100 | |
High resolution limit [Å] | 1.600 | |
Rmerge | 0.057 * | 0.450 * |
Total number of observations | 311387 * | |
Number of reflections | 55534 * | |
Completeness [%] | 99.4 * | 99 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 21 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
2 | 1 | reservoir | ethylene glycol | 20 (%(v/v)) |