4KAG
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 I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Wavelength(s) | 0.97630 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 57.140, 57.140, 135.330 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.940 - 1.120 |
| R-factor | 0.14509 |
| Rwork | 0.144 |
| R-free | 0.16108 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4eul |
| RMSD bond length | 0.030 |
| RMSD bond angle | 2.715 |
| Data scaling software | SCALA (0.1.16) |
| Phasing software | PHASER (2.3.0) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 39.940 |
| High resolution limit [Å] | 1.120 |
| Number of reflections | 91397 |
| Completeness [%] | 97.3 |
| Redundancy | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 291 | 0.1 M Na cacodylate, 0.2 M NaCl, 1M Na citrate, pH 6.5, VAPOR DIFFUSION, temperature 291K |
