1WVE
p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-06-03 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.830, 118.600, 136.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.850 |
| Rwork | 0.159 |
| R-free | 0.19400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB code 1DII |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.067 | 0.285 |
| Number of reflections | 94080 | |
| <I/σ(I)> | 18.6 | 2.1 |
| Completeness [%] | 90.9 | 52.3 |
| Redundancy | 5.1 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 296 | PEG 8000, Tris, ammonium acetate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K |
