1DAZ
Structural and kinetic analysis of drug resistant mutants of HIV-1 protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 90 |
Detector technology | IMAGE PLATE |
Collection date | 1997-10-14 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.239, 58.192, 61.215 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.550 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 26.420 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.600 | 1.610 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.054 | 0.133 |
Number of reflections | 27073 | |
<I/σ(I)> | 12.6 | |
Completeness [%] | 99.4 | 93.9 |
Redundancy | 6.4 | 5.96 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 5.6 | 297 | CITRATE/PHOSPHATE BUFFER 0.05M, DTT 10MM, DMSO 10%, SATURATED AMMONIUM SULPHATE 25-50%, PROTEIN 2-5 MG/ML, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4.5-8.0 (mg/ml) | |
2 | 1 | drop | sodium acetate | 20-50 (mM) | |
3 | 1 | reservoir | sodium citrate | 0.25 (M) | |
4 | 1 | reservoir | sodium phosphate | 0.5 (M) | |
5 | 1 | reservoir | ammonium sulfate | 20-45 (%sat) |