1VFQ
The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Collection date | 2003-06-17 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 25.610, 55.158, 37.426 |
Unit cell angles | 90.00, 95.96, 90.00 |
Refinement procedure
Resolution | 23.120 - 1.900 |
R-factor | 0.168 |
Rwork | 0.166 |
R-free | 0.21800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.660 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.262 | |
Number of reflections | 7524 | |
<I/σ(I)> | 13.8 | |
Completeness [%] | 91.5 | 91.5 |
Redundancy | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 30% PEG4000, 0.1M Tris-HCL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |