5EX6
Structure of P450 StaH from glycopeptide antibiotic A47934 biosynthesis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-05-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0039 |
| Spacegroup name | P 65 |
| Unit cell lengths | 109.520, 109.520, 187.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.400 - 2.400 |
| R-factor | 0.20072 |
| Rwork | 0.196 |
| R-free | 0.24728 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lfk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.080 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.400 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.099 | 0.403 |
| Number of reflections | 47412 | |
| <I/σ(I)> | 14.7 | 4 |
| Completeness [%] | 95.4 | 88.9 |
| Redundancy | 4.5 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 0.2 M (NH4)3 citrate pH 7.0, 16.0% (w/v) PEG 3350 |
