1T3Y
Three Crystal Structures of Human Coactosin-like Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BSRF BEAMLINE 3W1A |
Synchrotron site | BSRF |
Beamline | 3W1A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-03-31 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 28.027, 55.382, 70.792 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.150 |
R-factor | 0.1189 |
Rwork | 0.119 |
R-free | 0.15850 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.014 |
RMSD bond angle | 0.032 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.180 |
High resolution limit [Å] | 1.150 | 1.150 |
Rmerge | 0.067 | 0.406 |
Number of reflections | 37740 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | TRIS-HCL, NACL, IMIDAZOLE, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |