3KAK
Structure of homoglutathione synthetase from Glycine max in open conformation with gamma-glutamyl-cysteine bound.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-06-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.880, 80.950, 89.120 |
| Unit cell angles | 90.00, 95.96, 90.00 |
Refinement procedure
| Resolution | 19.800 - 2.110 |
| R-factor | 0.21064 |
| Rwork | 0.207 |
| R-free | 0.28797 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | homoglutathione synthetase apoenzyme |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.548 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.800 | 2.160 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 51043 | |
| <I/σ(I)> | 11.4 | 2.4 |
| Completeness [%] | 96.5 | 92.3 |
| Redundancy | 3.6 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 20% PEG3000, 0.1 M 3-(N-morpholino)-2-hydroxypropanesulfonic acid (MOPSO), pH 7, 0.2 M MgSO4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
