8FXS
Crystal structure of human pro-TGF-beta2 in complex with Nb9
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-1 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-09-02 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.92009 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.683, 89.554, 89.740 |
Unit cell angles | 90.00, 95.00, 90.00 |
Refinement procedure
Resolution | 48.270 - 3.150 |
R-factor | 0.2546 |
Rwork | 0.249 |
R-free | 0.30090 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.543 |
Data reduction software | XDS (20190417) |
Data scaling software | XDS (20190417) |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.270 | 3.263 |
High resolution limit [Å] | 3.150 | 3.150 |
Number of reflections | 18849 | 1881 |
<I/σ(I)> | 8.48 | |
Completeness [%] | 98.3 | 99.37 |
Redundancy | 3.4 | 3.6 |
CC(1/2) | 0.967 | 0.423 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | Crystals of the Nb9/proTGF-beta2 complex (1 microliter) were formed in hanging drops with 1 microliter of 100 mM HEPES pH 7.6, 10% PEG 4000. |