3AJN
Structural basis of glycine amide on suppression of protein aggregation by high resolution X-ray analysis
Replaces: 2ZXSExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL32B2 |
Synchrotron site | SPring-8 |
Beamline | BL32B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2010-05-25 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.000 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 78.510, 78.510, 36.962 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.050 |
R-factor | 0.14674 |
Rwork | 0.146 |
R-free | 0.16306 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 193l |
RMSD bond length | 0.020 |
RMSD bond angle | 2.006 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.090 |
High resolution limit [Å] | 1.050 | 1.050 |
Rmerge | 0.039 | 0.308 |
Number of reflections | 102269 | |
<I/σ(I)> | 5.5 | |
Completeness [%] | 94 | |
Redundancy | 6.8 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch | 4.5 | 293 | 0.05M sodium acetate, 1.0M glycine amide, pH 4.5, Batch, temperature 293K |