1RTD
STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 110 |
Detector technology | CCD |
Detector | BRANDEIS - B4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.840, 150.700, 280.880 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 3.200 |
R-factor | 0.224 |
Rwork | 0.224 |
R-free | 0.29800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 2.100 |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 3.300 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.103 * | 0.372 * |
Number of reflections | 54281 | 4802 * |
<I/σ(I)> | 11.2 | 2.7 |
Completeness [%] | 93.8 | 84.3 |
Redundancy | 4.2 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 4 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein-DNA complex | 8 (mg/ml) | |
10 | 1 | reservoir | 10 (mM) | ||
11 | 1 | reservoir | EDTA | 0.1 (mM) | |
2 | 1 | drop | MES | 10 (mM) | |
3 | 1 | drop | 2 (mM) | ||
4 | 1 | drop | 200 (mM) | ||
5 | 1 | drop | EDTA | 0.02 (mM) | |
6 | 1 | drop | dTTP | 2.5 (mM) | |
7 | 1 | reservoir | PEG6000 | 14 (%(w/v)) | |
8 | 1 | reservoir | MES | 50 (mM) | |
9 | 1 | reservoir | 1 (M) |