1SMI
A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-08-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.900 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 61.206, 118.929, 146.338 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.920 - 2.000 |
| R-factor | 0.22699 |
| Rwork | 0.224 |
| R-free | 0.28831 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jpz |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.719 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.9999) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.051 | 0.441 |
| Number of reflections | 68550 | |
| <I/σ(I)> | 28.2 | 2.41 |
| Completeness [%] | 94.0 | 97.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 277 | PEG 2000, MME, 10mM Manganese sulphate, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
