3AAC
Small heat shock protein hsp14.0 with the mutations of I120F and I122F in the form II crystal
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-05-21 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 41 |
Unit cell lengths | 69.564, 69.564, 49.724 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.970 - 2.400 |
Rwork | 0.245 |
R-free | 0.27500 |
Structure solution method | MIRAS |
RMSD bond length | 0.003 |
RMSD bond angle | 0.494 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 8995 | |
<I/σ(I)> | 16.1 | 2.7 |
Completeness [%] | 95.0 | 88.7 |
Redundancy | 4.6 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 290 | 40% ethylene glycol, 200mM zinc acetate, 100mM MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 290K |