4OBG
Crystal Structure of Nelfinavir-Resistant, Inactive HIV-1 Protease (D30N/N88D) in Complex with the p1-p6 substrate.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-09 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.672, 60.114, 60.196 |
| Unit cell angles | 90.00, 99.09, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.780 |
| R-factor | 0.20312 |
| Rwork | 0.200 |
| R-free | 0.25461 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t3r |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.404 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Number of reflections | 34288 | |
| <I/σ(I)> | 14.7 | 3.88 |
| Completeness [%] | 99.2 | 99.7 |
| Redundancy | 3.9 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 28% PEG 5000, 0.1M ammonium sulfate, 0.5M MES monohydrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
