1JLG
CRYSTAL STRUCTURE OF Y188C MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH UC-781
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-12-13 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 138.000, 109.800, 73.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.680 - 2.600 |
| R-factor | 0.214 * |
| Rwork | 0.220 |
| R-free | 0.29200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.061 | |
| Total number of observations | 94725 * | |
| Number of reflections | 33717 | 3210 * |
| <I/σ(I)> | 9.6 | 1.2 |
| Completeness [%] | 95.9 | 92.9 |
| Redundancy | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5 | 4 * | Stammers, D.K., (1994) J.Mol.Biol., 242, 586. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 26 (mg/ml) | |
| 2 | 1 | drop | PEG3400 | 6 (%(w/v)) | |
| 3 | 1 | drop | citrate/phosphate | ||
| 4 | 1 | reservoir | PEG3400 | 6 (%(w/v)) |
