4M91
crystal structure of hN33/Tusc3-peptide 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2010-03-10 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.769, 62.235, 64.551 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.880 - 1.100 |
R-factor | 0.1378 |
Rwork | 0.137 |
R-free | 0.16023 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4m8g |
RMSD bond length | 0.015 |
RMSD bond angle | 1.594 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 39.770 |
High resolution limit [Å] | 1.100 |
Number of reflections | 65763 |
<I/σ(I)> | 18.2 |
Completeness [%] | 96.2 |
Redundancy | 9.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 0.2 M KSCN, 10.5% PEG 8K, 10% PEG 1K in 100 mM cacodylic acid-NaOH, pH 6.5, VAPOR DIFFUSION, SITTING DROP |