1K35
Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.979151 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.038, 73.263, 92.354 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.200 |
R-factor | 0.23773 |
Rwork | 0.235 |
R-free | 0.27600 * |
Structure solution method | MAD |
RMSD bond length | 0.015 * |
RMSD bond angle | 1.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.071 * | 0.333 * |
Total number of observations | 185144 * | |
Number of reflections | 24319 | |
<I/σ(I)> | 27.8 | 5.8 |
Completeness [%] | 96.5 | 98.7 |
Redundancy | 7.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | Regni, C.A., (2000) Acta Crystallogr, D56, 761. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12-15 (mg/ml) | |
2 | 1 | drop | MOPS | 10 (mM) | pH7.0 |
3 | 1 | reservoir | sodium potassium tartrate | 1.4 (M) | |
4 | 1 | reservoir | sodium HEPES | 100 (mM) | pH7.5 |