5B2X
Crystal Structure of P450BM3 mutant with N-perfluoroheptanoyl-L-tryptophan
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.402, 147.355, 64.301 |
| Unit cell angles | 90.00, 100.10, 90.00 |
Refinement procedure
| Resolution | 19.170 - 1.900 |
| R-factor | 0.1813 |
| Rwork | 0.180 |
| R-free | 0.21570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wsp |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.207 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 4.090 | 1.900 |
| Rmerge | 0.067 | 0.025 | 0.362 |
| Number of reflections | 83890 | ||
| <I/σ(I)> | 10.1 | ||
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 3.7 | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.9 | 293 | 75mM Tris-HCl (pH7.9), 50uM N-perfluoroheptanoyl L-tryptophan, 0.5% (v/v) dimethyl sulfoxide, 100mM MgCl, 10.0% (w/v) PEG 8000 |
