4E8E
Structural characterization of Bombyx mori glutathione transferase BmGSTD1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.783, 88.756, 86.488 |
Unit cell angles | 90.00, 102.68, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.510 |
R-factor | 0.23239 |
Rwork | 0.230 |
R-free | 0.27556 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1r5a |
RMSD bond length | 0.006 |
RMSD bond angle | 0.853 |
Data reduction software | HKL-2000 |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.075 | 0.166 |
Number of reflections | 28461 | |
<I/σ(I)> | 19.2 | 7.4 |
Completeness [%] | 98.5 | 90.4 |
Redundancy | 3.7 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 289.15 | 8% PEG 4000, 0.1M sodium acetate trihydrate (pH 4.6) , VAPOR DIFFUSION, HANGING DROP, temperature 289.15K |