4AL2
peptide deformylase (Ni-form) with hydrosulfide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-08-25 |
| Detector | RIGAKU SATURN 92 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 142.206, 63.222, 118.175 |
| Unit cell angles | 90.00, 144.28, 90.00 |
Refinement procedure
| Resolution | 69.000 - 2.600 |
| R-factor | 0.2108 |
| Rwork | 0.206 |
| R-free | 0.29781 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w3t |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.441 |
| Data reduction software | d*TREK |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.220 | 0.520 |
| Number of reflections | 18933 | |
| <I/σ(I)> | 3.1 | 1.7 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 293 | 25% PEG 4000, 200 MM NAOAC PH 4.6, 293 K, INCUBATED IN H2S ATMOSPHERE EQUILIBRATED WITH 50 MM NA2S AT PH 4.6 |
