5FII
Structure of a human aspartate kinase, chorismate mutase and TyrA domain.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Collection date | 2014-05-23 |
| Spacegroup name | P 1 |
| Unit cell lengths | 36.140, 37.410, 64.080 |
| Unit cell angles | 98.94, 103.84, 94.79 |
Refinement procedure
| Resolution | 34.810 - 1.800 |
| R-factor | 0.17921 |
| Rwork | 0.177 |
| R-free | 0.22178 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.436 |
| Phasing software | Rosetta |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.810 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.060 | 0.500 |
| Number of reflections | 28770 | |
| <I/σ(I)> | 12 | 2.1 |
| Completeness [%] | 91.1 | 90.5 |
| Redundancy | 1.7 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 25% PEG 3350, 0.20M NACL, 0.1M BIS-TRIS PH 5.5 |
