1P5G
Enzyme-ligand complex of P. aeruginosa PMM/PGM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-02-08 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.591, 74.372, 85.994 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.600 * |
R-factor | 0.16177 |
Rwork | 0.160 |
R-free | 0.19000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k35 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.340 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.062 | 0.477 |
Number of reflections | 59418 | |
<I/σ(I)> | 41.8 | 5.6 |
Completeness [%] | 98.7 | 87.7 |
Redundancy | 12.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 293 | 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 |