5LFN
Crystal structure of human chondroadherin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-10-06 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.480, 111.590, 128.680 |
Unit cell angles | 90.00, 92.22, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.100 |
R-factor | 0.2457 |
Rwork | 0.245 |
R-free | 0.26230 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | DE NOVO MODELS |
RMSD bond length | 0.002 |
RMSD bond angle | 0.589 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | AMPLE |
Refinement software | PHENIX ((1.11rc2_2531: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.088 | 0.697 |
Number of reflections | 88893 | |
<I/σ(I)> | 6.7 | 1.1 |
Completeness [%] | 95.8 | 91.1 |
Redundancy | 2.4 | 2 |
CC(1/2) | 0.994 | 0.562 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 9.5 | 293 | 21% PEG 3350, 6% xylitol, 0.1 M glycine-NaOH pH 9.5-10.5, 0.2 M ammonium sulfate. Protein at 1.2 mg/ml in 20 mM Tris pH 7.0, 200 mM NaCl. Mixed in 1:1 ratio with reservoir. |