5QU5
Domain Swap in the first SH3 domain of human Nck1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-04-10 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.99994 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.200, 55.170, 55.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.030 - 1.110 |
R-factor | 0.1551 |
Rwork | 0.152 |
R-free | 0.20790 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.022 |
RMSD bond angle | 2.037 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.030 | 39.030 | 1.130 |
High resolution limit [Å] | 1.100 | 4.920 | 1.100 |
Rmerge | 0.077 | 0.029 | 13.661 |
Rmeas | 0.083 | 0.031 | 14.734 |
Total number of observations | 351842 | ||
Number of reflections | 48767 | 643 | 3396 |
<I/σ(I)> | 8.16 | 41.65 | 0.1 |
Completeness [%] | 96.4 | 99.2 | 92.2 |
Redundancy | 7.215 | 6.782 | 7.101 |
CC(1/2) | 0.999 | 1.000 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 5-20 mg/mL protein in 25mM HEPES\/NaOH pH7.8, 150mM NaCl mixed 60-70% with 40-30% reservoir consisting of 0.1M Bis-Tris/HCl pH5.5, 2M NaCl, 25% PEG3350 |