6JZ1
Apo structure of b-glucuronidase from Ruminococcus gnavus at 1.7 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13C1 |
Synchrotron site | NSRRC |
Beamline | BL13C1 |
Temperature [K] | 277 |
Detector technology | CCD |
Collection date | 2018-10-16 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 163.008, 103.128, 112.617 |
Unit cell angles | 90.00, 130.96, 90.00 |
Refinement procedure
Resolution | 29.710 - 1.730 |
R-factor | 0.308 |
Rwork | 0.116 |
R-free | 0.19200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5z19 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (19-1692) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 10.000 | 1.790 |
High resolution limit [Å] | 1.730 | 3.730 | 1.730 |
Rmerge | 0.062 | 0.034 | 0.564 |
Rmeas | 0.072 | 0.039 | 0.657 |
Rpim | 0.036 | 0.020 | 0.332 |
Total number of observations | 566535 | ||
Number of reflections | 144698 | 14339 | 14423 |
<I/σ(I)> | 9.9 | ||
Completeness [%] | 99.2 | 97 | 99.5 |
Redundancy | 3.9 | 4 | 3.7 |
CC(1/2) | 0.997 | 0.759 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 70% MPD, 0.1 M HEPES, pH 7.5, 0.2 M CaCl2 |