7RG8
Crystal Structure of a Stable Heparanase Mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-02-09 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.785, 76.094, 124.432 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.010 - 1.300 |
R-factor | 0.1439 |
Rwork | 0.143 |
R-free | 0.16500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5e8m |
Data reduction software | DIALS |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 53.890 | 53.890 | 1.320 |
High resolution limit [Å] | 1.300 | 7.120 | 1.300 |
Rmerge | 0.073 | 0.061 | 1.317 |
Rmeas | 0.076 | 0.064 | 1.385 |
Rpim | 0.021 | 0.021 | 0.421 |
Total number of observations | 1829452 | 11032 | 72198 |
Number of reflections | 139784 | 994 | 6775 |
<I/σ(I)> | 14.9 | 37.4 | 1.3 |
Completeness [%] | 99.9 | 99.4 | 99.2 |
Redundancy | 13.1 | 11.1 | 10.7 |
CC(1/2) | 0.998 | 0.980 | 0.851 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | 0.2M Ammonium Sulfate, Sodium Acetate pH 5.5, 20% PEG 4000 |