2GM8
TenA Homolog/Thi-4 Thiaminase complexed with product 4-amino-5-hydroxymethyl-2-methylpyrimidine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-04 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.647, 94.287, 73.198 |
| Unit cell angles | 90.00, 113.65, 90.00 |
Refinement procedure
| Resolution | 67.120 - 2.500 |
| R-factor | 0.189 |
| Rwork | 0.187 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ID 2GM7 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.308 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 80.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.110 | 0.299 |
| Number of reflections | 32375 | 3175 |
| <I/σ(I)> | 13 | |
| Completeness [%] | 99.0 | 98.3 |
| Redundancy | 2.9 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 18 mg/mL protein was complexed with thiamine diphosphate and enzyme mediated catalysis produced 4-amino-5-hydroxymethyl-2-methylpyrimidine. Reservoir contains 20% PEG 8000, 0.1M Tris pH 8.5, 0.2M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
