1K1T
Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2000-10-20 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.256, 58.130, 61.563 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.200 |
| R-factor | 0.1957 |
| Rwork | 0.196 |
| R-free | 0.22700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 0.028 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 * | 1.230 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.046 * | 0.155 |
| Number of reflections | 50107 | |
| Completeness [%] | 86.2 | 50.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 20-50% Saturated Ammonium Sulphate, 10% DMSO, 0.25M citrate/0.5M phosphate buffer, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | citrate | 0.25 (M) | |
| 2 | 1 | reservoir | phosphate | 0.5 (M) | pH5-6.5 |
| 3 | 1 | reservoir | DMSO | 10 (%) | |
| 4 | 1 | reservoir | dithiothreitol | 10 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 20-50 (%sat) | |
| 6 | 1 | drop | protein | 2-10 (mg/ml) |
