1NWR
Crystal structure of human cartilage gp39 (HC-gp39)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 43 |
Unit cell lengths | 127.300, 127.300, 107.760 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 * - 2.600* |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.24000 * |
Structure solution method | MIR |
RMSD bond length | 0.008 |
RMSD bond angle | 23.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.060 * | 0.259 |
Total number of observations | 205355 * | |
Number of reflections | 52490 | |
<I/σ(I)> | 18.2 | 4.1 |
Completeness [%] | 99.6 * | 96.2 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.2 * | 277 | PEG8000, NaCl, Na-citrate buffer, pH 5.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 5.10 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4 (mg/ml) | |
2 | 1 | drop | 1 (M) | ||
3 | 1 | drop | BES | 10 (mM) | pH7.2 |
4 | 1 | reservoir | PEG8000 | 10 (%) | |
5 | 1 | reservoir | 0.5 (M) | ||
6 | 1 | reservoir | sodium citrate | 0.1 (M) | pH5.1 |