9LSA
Crystal structure of mRFP1 with a grafted calcium-binding sequence and one bound calcium ion in a calcium-containing solution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-01-30 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.270, 86.080, 109.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.100 - 1.620 |
| R-factor | 0.1743 |
| Rwork | 0.174 |
| R-free | 0.18910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.967 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.17.1_3660: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.100 | 1.720 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Number of reflections | 68728 | 11150 |
| <I/σ(I)> | 22.9 | 1.88 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.88 | 7.02 |
| CC(1/2) | 1.000 | 0.740 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1M Tris-HCl pH 8.5, 0.1M CaCl2, 30% (w/v) PEG 4000 |
