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 |