1MRL
Crystal structure of streptogramin A acetyltransferase with dalfopristin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-03-11 |
Detector | MARRESEARCH |
Wavelength(s) | 0.8700 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 82.914, 90.905, 104.529 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 * - 2.800 |
R-factor | 0.2723 |
Rwork | 0.271 |
R-free | 0.30300 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mr7 |
RMSD bond length | 0.003 |
RMSD bond angle | 1.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.870 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.082 | 0.358 |
Total number of observations | 222509 * | |
Number of reflections | 20118 | |
<I/σ(I)> | 15.5 | 3.6 |
Completeness [%] | 99.7 * | 99.2 * |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 290 | 0.2M Sodium Fluoride, 20% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 0.25 (mM) | |
2 | 1 | drop | dalfopristin | 1.5 (mM) | |
3 | 1 | reservoir | sodium fluoride | 0.2 (M) | |
4 | 1 | reservoir | PEG3350 | 20 (%(w/v)) |