1KOU
Crystal Structure of the Photoactive Yellow Protein Reconstituted with Caffeic Acid at 1.16 A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X26C |
| Synchrotron site | NSLS |
| Beamline | X26C |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-01-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.08 |
| Spacegroup name | P 65 |
| Unit cell lengths | 40.582, 40.582, 117.801 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 * - 1.160 |
| R-factor | 0.162 * |
| Rwork | 0.162 |
| R-free | 0.20300 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2phy |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.120 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.200 |
| High resolution limit [Å] | 1.160 | 1.160 |
| Rmerge | 0.040 | 0.546 |
| Total number of observations | 333681 * | |
| Number of reflections | 36609 | 3352 * |
| <I/σ(I)> | 15.7 | 2.7 |
| Completeness [%] | 96.7 | 89.4 |
| Redundancy | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6.5 | 290 | PEGMME 2000, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 25 (mg/ml) | |
| 2 | 1 | reservoir | PEG2000 MME | ||
| 3 | 1 | reservoir | MES | 50 (mM) | pH6.5 |
