5YHS
Pyruvylated beta-D-galactosidase from Bacillus sp. HMA207, apo form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-14 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 1.0000 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 113.997, 113.997, 148.678 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 98.720 - 2.500 |
R-factor | 0.22237 |
Rwork | 0.219 |
R-free | 0.27625 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ta9 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.643 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.073 | 0.989 |
Number of reflections | 39354 | 1925 |
<I/σ(I)> | 19.5 | 1.7 |
Completeness [%] | 100.0 | 100 |
Redundancy | 9.1 | 9.1 |
CC(1/2) | 0.777 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.2 | 293 | 50% PEG300, 0.1M phosphate-citrate buffer |