3OBA
Structure of the beta-galactosidase from Kluyveromyces lactis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 140.030, 153.340, 216.160 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.570 - 2.750 |
| R-factor | 0.2085 |
| Rwork | 0.207 |
| R-free | 0.24350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yq2 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.108 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 125.067 | 62.534 | 2.900 |
| High resolution limit [Å] | 2.750 | 8.700 | 2.750 |
| Rmerge | 0.172 | 0.053 | 0.536 |
| Total number of observations | 28971 | 123972 | |
| Number of reflections | 121272 | ||
| <I/σ(I)> | 10.7 | 12.2 | 1.4 |
| Completeness [%] | 100.0 | 99.7 | 100 |
| Redundancy | 7.2 | 7 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 24 % Polyethylen Glycol (PEG) 3350, 0.1 M BisTris pH 7.5, 0.2 M Sodium Tartrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
