1YDH
X-ray structure of a lysine decarboxylase-like protein from arabidopsis thaliana gene at5g11950
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 | C 1 2 1 |
| Unit cell lengths | 121.589, 80.427, 50.709 |
| Unit cell angles | 90.00, 102.97, 90.00 |
Refinement procedure
| Resolution | 35.450 - 2.152 |
| R-factor | 0.16164 |
| Rwork | 0.159 |
| R-free | 0.21300 |
| Structure solution method | SAD |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.939 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE (2.06) |
| Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.451 | 50.000 | 2.230 |
| High resolution limit [Å] | 2.152 | 4.740 | 2.150 |
| Rmerge | 0.384 | 0.119 | 0.384 |
| Total number of observations | 2537 | 2460 | |
| Number of reflections | 25771 | ||
| <I/σ(I)> | 6.266 | 2.401 | |
| Completeness [%] | 99.9 | 99.6 | 100 |
| Redundancy | 6.9 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 293 | 10 MG/ML PROTEIN, 13% MPEG 2K, 0.28 M POTASSIUM NITRATE, 0.1 M MOPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 7.00 |






