4KEX
Crystal structure analysis of a single amino acid deletion mutation in EGFP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Wavelength(s) | 0.97630 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.450, 63.140, 65.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.570 - 1.600 |
| R-factor | 0.1837 |
| Rwork | 0.182 |
| R-free | 0.20920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4eul |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.139 |
| Data scaling software | SCALA (0.1.16) |
| Phasing software | PHASER (2.5.1) |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 51.450 |
| High resolution limit [Å] | 1.600 |
| Rmerge | 0.092 |
| Number of reflections | 28209 |
| <I/σ(I)> | 15.2 |
| Completeness [%] | 98.1 |
| Redundancy | 7.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 4 | 291 | 0.1 M MMT Buffer (Malic acid, MES and Tris), 25% (w/v) PEG 1500, pH 4.0, VAPOR DIFFUSION, temperature 291K |






