1WVF
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 | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-06-27 |
Detector | SBC |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 88.640, 116.910, 50.220 |
Unit cell angles | 90.00, 113.18, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.300 |
Rwork | 0.146 |
R-free | 0.16700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB code 1DII |
RMSD bond length | 0.011 |
RMSD bond angle | 1.630 |
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 | 1.350 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.089 | 0.155 |
Number of reflections | 100440 | |
<I/σ(I)> | 19.6 | 4.1 |
Completeness [%] | 87.3 | 46.1 |
Redundancy | 4.3 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 296 | PEG 1500, acetate, magnesium acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K |