5KIL
CmlA beta-hydroxylase E377D mutant
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 | 2015-07-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97933 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 153.954, 153.954, 92.548 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.490 - 2.720 |
R-factor | 0.205 |
Rwork | 0.202 |
R-free | 0.26200 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 4jo0 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.969 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | REFMAC (5.7.0029) |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.500 | 2.770 |
High resolution limit [Å] | 2.720 | 2.720 |
Rmerge | 0.102 | 0.471 |
Number of reflections | 30307 | |
<I/σ(I)> | 29 | 4.8 |
Completeness [%] | 99.8 | 99.9 |
Redundancy | 7.2 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | PEG 20000, potassium acetate, HEPES, glycerol |