4KA9
Crystal structure analysis of single amino acid deletion mutations in EGFP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Wavelength(s) | 0.97630 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 91.870, 66.660, 45.290 |
| Unit cell angles | 90.00, 108.76, 90.00 |
Refinement procedure
| Resolution | 42.880 - 1.580 |
| R-factor | 0.1753 |
| Rwork | 0.173 |
| R-free | 0.21010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.318 |
| Data scaling software | SCALA (0.1.16) |
| Phasing software | PHASER (2.3.0) |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 43.490 |
| High resolution limit [Å] | 1.580 |
| Number of reflections | 34564 |
| Completeness [%] | 97.5 |
| Redundancy | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7 | 291 | 0.1 M HEPES, 0.01 M ZnCl2, 20% (w/v) PEG 6000, pH 7.0, vapor diffusion, temperature 291K |
