1KYS
Crystal Structure of a Zn-bound Green Fluorescent Protein Biosensor
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 | IMAGE PLATE |
| Collection date | 2000-12-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.147, 62.226, 68.817 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.440 |
| R-factor | 0.157 |
| Rwork | 0.157 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ema |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.028 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELX |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | 1.490 |
| High resolution limit [Å] | 1.440 | 1.440 |
| Rmerge | 0.054 * | 0.316 * |
| Total number of observations | 115486 * | |
| Number of reflections | 38864 * | |
| <I/σ(I)> | 23.4 | 2.4 |
| Completeness [%] | 95.5 | 79.2 |
| Redundancy | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | used microseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 50 (mM) | pH8.0 |
| 3 | 1 | reservoir | 50 (mM) | ||
| 4 | 1 | reservoir | PEG4000 | 19 (%) |
