1LM4
Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-08-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.224, 76.703, 112.116 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 * - 1.450 |
Rwork | 0.170 |
R-free | 0.20000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bs4 |
RMSD bond length | 0.015 |
RMSD bond angle | 24.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 * | 1.540 |
High resolution limit [Å] | 1.450 * | 1.450 |
Rmerge | 0.055 * | 0.154 * |
Number of reflections | 61791 | |
<I/σ(I)> | 16.8 | |
Completeness [%] | 99.1 | 95.6 |
Redundancy | 18.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 * | 20 * | PEG 6000, 0.1 M citric acid pH 5.0, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 27 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 30 (%(w/v)) | |
3 | 1 | reservoir | citric acid | 0.1 (M) | pH5.0 |