1K2B
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] | 90 |
| Detector technology | CCD |
| Collection date | 1999-10-08 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.037 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.759, 57.541, 60.841 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.700 |
| Rwork | 0.215 |
| R-free | 0.27500 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1daz |
| RMSD bond length | 0.011 |
| RMSD bond angle | 2.183 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 8.000 * | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.042 | 0.248 |
| Number of reflections | 20000 | |
| <I/σ(I)> | 10.8 | 5.1 |
| Completeness [%] | 99.0 | 98.4 |
| Redundancy | 4.1 |
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) |
