1EM9
ROUS SARCOMA VIRUS CAPSID PROTEIN: N-TERMINAL DOMAIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 113 |
Detector technology | IMAGE PLATE |
Collection date | 1998-07-03 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.500, 64.500, 108.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 55.500 - 2.050 |
Rwork | 0.247 |
R-free | 0.27100 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 19.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.000 | 2.110 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.049 | 0.335 |
Number of reflections | 17194 | |
Completeness [%] | 92.5 | 89.8 |
Redundancy | 5 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8 * | 4 * | Boric acid/Potassium Hydroxide, PEG 6000, Magnesium Nitrate, pH 9.1, VAPOR DIFFUSION, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20-30 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | reservoir | boric acid/KOH | 0.15 (M) | |
5 | 1 | reservoir | PEG6000 | 16-22 (%(v/v)) | |
6 | 1 | reservoir | 0.7 (M) |