1SSG
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-05-20 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 88.327, 88.327, 163.874 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.960 - 2.900 |
R-factor | 0.20663 |
Rwork | 0.205 |
R-free | 0.24433 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 8tim |
RMSD bond length | 0.012 |
RMSD bond angle | 1.328 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.089 | 0.600 |
Number of reflections | 16663 | |
<I/σ(I)> | 25 | 3.4 |
Completeness [%] | 99.7 | 97.4 |
Redundancy | 5.11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 294 | Citrate, ammonium sulphate, sodium chloride, 2-phosphoglycolate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |