1ROC
Crystal structure of the histone deposition protein Asf1
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2003-06-30 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.956, 0.920 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 94.395, 31.702, 53.625 |
Unit cell angles | 90.00, 124.55, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.500 |
R-factor | 0.20012 |
Rwork | 0.198 |
R-free | 0.24650 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.094 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.460 |
High resolution limit [Å] | 1.400 | 1.400 |
Number of reflections | 23670 | |
<I/σ(I)> | 18.8 | 1.9 |
Completeness [%] | 92.2 | 48 |
Redundancy | 3.3 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 18 * | PEG 3350, sodium bromide, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | HEPES-NaOH | 10 (mM) | pH7.5 |
10 | 1 | reservoir | Asf1N | 900nl | |
2 | 1 | drop | 50 (mM) | ||
3 | 1 | drop | TCEP | 1 (mM) | |
4 | 1 | drop | 100 (mM) | ||
5 | 1 | drop | 100 (mM) | ||
6 | 1 | drop | PEG3350 | 20 (%) | |
7 | 1 | drop | Asf1N | 800nl | |
8 | 1 | reservoir | 0.85-1.0 (M) | ||
9 | 1 | reservoir | PEG3350 | 17 (%) |