6AN3
Crystal structure of H172A-peptidylglycine alpha-hydroxylating monooxygenase (PHM) mutant soaked with peptide (no CuH bound, no peptide bound)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E DW |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-05 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.029, 66.847, 70.246 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.430 - 2.050 |
R-factor | 0.2011 |
Rwork | 0.197 |
R-free | 0.28170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1phm |
RMSD bond length | 0.016 |
RMSD bond angle | 1.874 |
Data scaling software | SCALEPACK |
Phasing software | REFMAC |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.090 |
High resolution limit [Å] | 2.050 | 5.560 | 2.050 |
Rmerge | 0.051 | 0.043 | 0.145 |
Rmeas | 0.055 | 0.047 | 0.186 |
Rpim | 0.022 | 0.020 | 0.114 |
Total number of observations | 93871 | ||
Number of reflections | 17232 | 1001 | 623 |
<I/σ(I)> | 20.8 | ||
Completeness [%] | 95.6 | 99.3 | 70.6 |
Redundancy | 5.4 | 5.3 | 2 |
CC(1/2) | 0.998 | 0.955 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 293 | 19-24% PEG 4000, Tris HCL |