1H0X
Structure of Alba: an archaeal chromatin protein modulated by acetylation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Collection date | 2001-01-15 |
Detector | MSC |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 84.310, 84.310, 162.220 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.600 |
R-factor | 0.235 |
Rwork | 0.235 |
R-free | 0.28500 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.046 | 0.320 |
Number of reflections | 10996 | |
<I/σ(I)> | 6.9 | 2.7 |
Completeness [%] | 98.0 | 94.7 * |
Redundancy | 7.6 | 7.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | Wardleworth, B.N., (2001) Acta Crystallogr.,Sect.D, 57, 1893. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | Tris | 50 (mM) | pH7.5 |
3 | 1 | drop | 300 (mM) | ||
4 | 1 | reservoir | PEG8000 | 18 (%) | |
5 | 1 | reservoir | sodium cacodylate | 0.1 (M) | pH6.5 |
6 | 1 | reservoir | 0.2 (M) | ||
7 | 1 | reservoir | 1,2,3-heptanetriol | 0.1 (M) |