1D2M
UVRB PROTEIN OF THERMUS THERMOPHILUS HB8; A NUCLEOTIDE EXCISION REPAIR ENZYME
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-06-20 |
| Detector | RIGAKU RAXIS |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 135.040, 135.040, 106.756 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.234 |
| Rwork | 0.234 |
| R-free | 0.25300 |
| RMSD bond length | 0.006 * |
| RMSD bond angle | 1.300 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.960 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.063 | 0.166 |
| Number of reflections | 82751 | |
| <I/σ(I)> | 21.5 | |
| Completeness [%] | 93.5 | 76 |
| Redundancy | 4 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 293 | Shibata, A., (1999) Acta Crystallogr.D55, 704. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | beta-mercaptoehtanol | 10 (mM) | |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | drop | glycerol | 10 (%(v/v)) | |
| 5 | 1 | drop | Tris-HCl | 50 (mM) | |
| 6 | 1 | reservoir | lithium sulfate | 1.78 (M) | |
| 7 | 1 | reservoir | beta-octylglucoside | 0.5 (%(w/v)) | |
| 8 | 1 | reservoir | MES | 100 (mM) |
