1LWC
CRYSTAL STRUCTURE OF M184V MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH NEVIRAPINE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID2 |
| Synchrotron site | ESRF |
| Beamline | ID2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-06-27 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.9903 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 140.000, 115.200, 65.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 2.620 |
| R-factor | 0.207 * |
| Rwork | 0.215 |
| R-free | 0.28000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.690 * |
| 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 | 2.710 |
| High resolution limit [Å] | 2.620 | 2.620 |
| Rmerge | 0.075 | |
| Total number of observations | 134485 * | |
| Number of reflections | 28631 | 2326 * |
| <I/σ(I)> | 17.7 | 2 |
| Completeness [%] | 86.8 | 71.6 |
| Redundancy | 4.7 |
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 | reservoir | PEG3400 | 6 (%(w/v)) | |
| 4 | 1 | drop | citrate/phosphate |
