3T9K
Crystal Structure of ACAP1 C-portion mutant S554D fused with integrin beta1 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-18 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 108.258, 164.871, 41.665 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.300 |
R-factor | 0.19056 |
Rwork | 0.189 |
R-free | 0.22540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3jue |
RMSD bond length | 0.012 |
RMSD bond angle | 1.351 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASES |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.240 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.410 | |
Number of reflections | 37309 | |
Completeness [%] | 97.3 | 83.8 |
Redundancy | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 289 | 0.2M ammonium sulfate, 14% PEG 3350, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K |