1NUI
Crystal Structure of the primase fragment of Bacteriophage T7 primase-helicase protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2002-07-05 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9474, 0.9797, 0.9795, 0.9300, 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 136.459, 136.460, 85.445 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.900 |
R-factor | 0.23665 |
Rwork | 0.235 |
R-free | 0.27600 * |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.460 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.1.19) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.056 * | 0.241 |
Number of reflections | 28599 | |
<I/σ(I)> | 14.7 | |
Completeness [%] | 98.6 | 93.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 22 * | Sodium Formate, MES, DTT, ATP, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | drop | MES | 50 (mM) | pH6.3 |
3 | 1 | drop | sodium formate | 2 (M) | |
4 | 1 | drop | dithiothreitol | 5.5 (mM) | |
5 | 1 | drop | ATP | 2.5 (mM) | |
6 | 1 | reservoir | MES | 100 (mM) | pH6.3 |
7 | 1 | reservoir | sodium formate | 4 (M) | |
8 | 1 | reservoir | dithiothreitol | 5.5 (mM) |