1D0E
CRYSTAL STRUCTURES OF THE N-TERMINAL FRAGMENT FROM MOLONEY MURINE LEUKEMIA VIRUS REVERSE TRANSCRIPTASE COMPLEXED WITH NUCLEIC ACID: FUNCTIONAL IMPLICATIONS FOR TEMPLATE-PRIMER BINDING TO THE FINGERS DOMAIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 108 |
Detector technology | IMAGE PLATE |
Collection date | 1999-05-15 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.160, 63.540, 73.500 |
Unit cell angles | 90.00, 103.85, 90.00 |
Refinement procedure
Resolution | 20.000 * - 3.000 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.29800 |
RMSD bond length | 0.011 |
RMSD bond angle | 24.460 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 500.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.149 | 0.314 |
Total number of observations | 35570 * | |
Number of reflections | 11540 | |
<I/σ(I)> | 5.95 | |
Completeness [%] | 95.7 | 92.2 |
Redundancy | 3.1 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | used to seeding, Sun, D., (1998) Protein Sci., 7, 1575. * |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | NH4CL | ||
2 | 1 | 1 | HEPES | ||
3 | 1 | 1 | PEG 4000 | ||
4 | 1 | 2 | PEG 4000 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | HEPES | 100 (mM) | |
2 | 1 | reservoir | PEG4000 | 13 (%) | |
3 | 1 | reservoir | 75 (mM) |