6U1A
Crystal Structure of Fluorescent Protein FusionRed
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-03-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.015, 55.261, 89.347 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.520 - 1.090 |
| R-factor | 0.1271 |
| Rwork | 0.127 |
| R-free | 0.14670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bxa |
| RMSD bond length | 0.027 |
| RMSD bond angle | 2.559 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.130 |
| High resolution limit [Å] | 1.090 | 2.350 | 1.090 |
| Rmerge | 0.050 | 0.036 | 0.568 |
| Rmeas | 0.054 | 0.039 | 0.623 |
| Rpim | 0.020 | 0.015 | 0.250 |
| Total number of observations | 633565 | ||
| Number of reflections | 92579 | 9552 | 8578 |
| <I/σ(I)> | 12.2 | ||
| Completeness [%] | 98.8 | 97.3 | 92.5 |
| Redundancy | 6.8 | 6.8 | 5.5 |
| CC(1/2) | 0.998 | 0.846 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 5 mM CoCl2, 5 mM NiCl2, 5mM CdCl2, 5mM MgCl2, 0.1 M HEPES pH 7.5, 12% PEG3350 |
