1Z84
X-ray structure of galt-like protein from arabidopsis thaliana at5g18200
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-12-15 |
| Detector | APS-1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.037, 95.650, 110.918 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.280 - 1.830 |
| R-factor | 0.18833 |
| Rwork | 0.186 |
| R-free | 0.23100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1VKV |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.558 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.486 | 1.900 |
| High resolution limit [Å] | 1.834 | 1.830 |
| Rmerge | 0.083 | 0.386 |
| Number of reflections | 57501 | |
| <I/σ(I)> | 15.249 | 4.543 |
| Completeness [%] | 96.5 | 71.4 |
| Redundancy | 6.9 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 293 | 10 MG/ML PROTEIN, 20% PEG 2000, 0.2M Sodium Chloride, 0.10M MES-Acetate, vapor diffusion, hanging drop, temperature 293K, pH 5.50 |






