6LYW
Structural insight into the biological functions of Arabidopsis thaliana ACHT1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | LIQUID ANODE |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-04-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 102.686, 100.560, 92.801 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.403 - 1.700 |
| R-factor | 0.1534 |
| Rwork | 0.152 |
| R-free | 0.17250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zzx |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.031 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 3.660 | 1.700 |
| Rmerge | 0.064 | 0.032 | 0.695 |
| Rmeas | 0.072 | 0.036 | 0.775 |
| Rpim | 0.031 | 0.016 | 0.334 |
| Total number of observations | 253890 | ||
| Number of reflections | 52610 | 5327 | 5231 |
| <I/σ(I)> | 9.7 | ||
| Completeness [%] | 99.4 | 96.2 | 100 |
| Redundancy | 4.8 | 4.6 | 4.9 |
| CC(1/2) | 0.998 | 0.854 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | ammonium sulfate, isopropanol,agarose |
