5VG0
Room temperature X-ray crystallographic structure of a Jonesia denitrificans lytic polysaccharide monooxygenase at 1.1 angstrom resolution.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 295 |
Detector technology | CMOS |
Collection date | 2015-05-27 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 32.040, 75.560, 120.360 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.000 - 1.100 |
R-factor | 0.114 |
Rwork | 0.114 |
R-free | 0.12800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5aa7 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.975 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.000 | 1.160 |
High resolution limit [Å] | 1.100 | 1.100 |
Number of reflections | 1248110 | |
<I/σ(I)> | 13.7 | |
Completeness [%] | 97.3 | 95 |
Redundancy | 10.7 | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | Purified enzyme was incubated with a threefold molar excess of CuSO4 for 30 min at room temperature. To remove excess copper, the protein was loaded onto a desalting column equilibrated with 20 mM Tris-HCl pH 8.0. 30 ul protein solution at 48 mg/ml was mixed with 30 ul reservoir buffer consisting of 1.9 M DL-malic acid pH 7.0 |