5GHF
Transaminase with L-ala
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 5C (4A) |
| Synchrotron site | PAL/PLS |
| Beamline | 5C (4A) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-28 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 78.800, 102.000, 116.730 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.530 - 2.000 |
| R-factor | 0.13708 |
| Rwork | 0.135 |
| R-free | 0.17426 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.869 |
| Data reduction software | HKL-2000 |
| Data scaling software | Aimless |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 27.530 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.147 |
| Number of reflections | 58830 |
| <I/σ(I)> | 11.9 |
| Completeness [%] | 96.5 |
| Redundancy | 10.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 8.5 | 290 | 0.1M Tris-HCl pH 8.5, 23% PEG 3350 |






