2BF3
Crystal structure of a toluene 4-monooxygenase catalytic effector protein variant missing ten N-terminal residues (delta-N10 T4moD)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-08-08 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 86.748, 86.748, 86.748 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 16.000 - 1.960 |
| R-factor | 0.204 |
| Rwork | 0.198 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NATIVE TOLUENE-4-MONOOXYGENASE CATALYTIC EFFECTOR |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.718 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 16.000 | 2.070 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Rmerge | 0.060 | 0.320 |
| Number of reflections | 15889 | |
| <I/σ(I)> | 9.6 | 2.3 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 21.4 | 21 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | PROTEIN WAS CRYSTALLIZED FROM 2.0 M AMMONIUM SULFATE, 5% (V/V) 2-PROPANOL, AND 1.5% (V/V) 1,2,3-HEPTANETRIOL |
