1C1K
BACTERIOPHAGE T4 GENE 59 HELICASE ASSEMBLY PROTEIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Temperature [K] | 90 |
Detector technology | IMAGE PLATE |
Collection date | 1998-01-27 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 31.865, 65.882, 108.166 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 5.000 - 1.450 |
R-factor | 0.205 |
Rwork | 0.200 |
R-free | 0.25300 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.050 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.500 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.038 * | 0.073 |
Total number of observations | 150823 * | |
Number of reflections | 37155 | |
<I/σ(I)> | 26.9 | |
Completeness [%] | 89.8 | 71.8 |
Redundancy | 3.95 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 4 * | 100 MM NA CACODYLATE, PH 6.5 200 MM NH4 ACETATE, 50 MM (NH4)2SO4, 10 - 14% PEG 3350 GRADIENT, 20% ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
10 | 1 | reservoir | ethylene glycol | 20 (%(w/v)) | |
2 | 1 | drop | bis-Tris-HCl | 50 (mM) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | 10 (mM) | ||
5 | 1 | drop | dithiothreitol | 1 (mM) | |
6 | 1 | reservoir | Na cacodylate | 100 (mM) | |
7 | 1 | reservoir | ammonium acetate | 200 (mM) | |
8 | 1 | reservoir | ammonium sulfate | 50 (mM) | |
9 | 1 | reservoir | PEG3350 | 14 (%(w/v)) |