6LCK
TtGalA, alpha-galactosidase from Thermus thermophilus in complex with p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-07-14 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9762 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 118.631, 205.288, 163.898 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.060 - 2.850 |
| R-factor | 0.1757 |
| Rwork | 0.174 |
| R-free | 0.22240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | apo structure |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.058 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.950 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.100 | 0.505 |
| Number of reflections | 46936 | 4617 |
| <I/σ(I)> | 19.9 | |
| Completeness [%] | 99.9 | |
| Redundancy | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 283 | 0.1M CAPSO pH 9.2, 0.2M Li2SO4, 10% PEG 3000 |
