7B2K
Structure of the M298F mutant of the Streptomyces coelicolor small laccase T1 copper axial ligand.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-04-18 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.97820 |
Spacegroup name | P 21 3 |
Unit cell lengths | 177.620, 177.620, 177.620 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.200 - 2.200 |
R-factor | 0.1716 |
Rwork | 0.171 |
R-free | 0.18510 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cg8 |
Data reduction software | XDS (VERSION Jan 26, 2018) |
Data scaling software | XSCALE (VERSION Jan 26, 2018) |
Phasing software | PHASER (2.8.2) |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.200 | 29.200 | 2.260 |
High resolution limit [Å] | 2.200 | 9.840 | 2.200 |
Rmerge | 0.085 | 0.044 | 0.805 |
Rmeas | 0.090 | 0.047 | 0.907 |
Total number of observations | 808727 | ||
Number of reflections | 92609 | 1100 | 5982 |
<I/σ(I)> | 16.5 | 39.55 | 1.69 |
Completeness [%] | 98.1 | 95.2 | 86.3 |
Redundancy | 8.733 | 8.583 | 4.309 |
CC(1/2) | 0.999 | 0.998 | 0.652 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Protein concentration was 20 mg/mL in 20 mM Tris-HCl buffer (pH 7.5). Mother liquor was made up of 40% MPD, 200 mM NH4-OAc and 100 mM HEPES (pH 7.5). The protein was mixed in 2:1 ratio with protein to mother liquor. |