1TDQ
Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-02-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.097 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 112.520, 86.420, 57.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.000 - 2.600 |
R-factor | 0.20995 |
Rwork | 0.209 |
R-free | 0.23441 |
Structure solution method | MIRAS |
RMSD bond length | 0.012 |
RMSD bond angle | 1.296 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | SHARP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.000 | 2.710 |
High resolution limit [Å] | 2.570 | 2.570 |
Number of reflections | 18210 | |
<I/σ(I)> | 7.2 | 3.4 |
Completeness [%] | 97.3 | 91.7 |
Redundancy | 8.7 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 294 | 8-12% PEG 8000, 150mM calcium acetate, 2-4% PEG MME 750, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |