1IO0
CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-10-13 |
Detector | MARRESEARCH |
Wavelength(s) | 0.7 |
Spacegroup name | H 3 |
Unit cell lengths | 69.294, 69.294, 101.223 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.450 |
Rwork | 0.203 |
R-free | 0.22000 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 24.073 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.500 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.076 | 0.286 |
Total number of observations | 357913 * | |
Number of reflections | 31954 | |
<I/σ(I)> | 13.4 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | 22 * | PEG 400, zinc sulfate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | glycine | 25 (mM) | pH3.0 |
3 | 1 | drop | MES-NaOH | 0.1 (M) | pH6.5 |
4 | 1 | drop | PEG400 | 24 (%(v/v)) | |
5 | 1 | drop | 10 (mM) | ||
6 | 1 | reservoir | MES- NaOH | 0.1 (M) | pH6.5 |
7 | 1 | reservoir | PEG400 | 15 (%(v/v)) | |
8 | 1 | reservoir | 6 (mM) |