2R0L
Short Form HGFA with Inhibitory Fab75
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 |
Unit cell lengths | 38.820, 48.230, 97.050 |
Unit cell angles | 98.39, 96.24, 100.77 |
Refinement procedure
Resolution | 47.510 - 2.200 |
R-factor | 0.19537 |
Rwork | 0.193 |
R-free | 0.24797 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | pdb 1YC0 pdb 1FVD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.164 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.1.07) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.048 | 0.212 |
Number of reflections | 32514 | |
<I/σ(I)> | 3 | 3 |
Completeness [%] | 94.4 | 74.5 |
Redundancy | 1.9 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 1:1 mixture of protein complex solution at 15 mg/mL and reservoir containing 20% PEG 10000, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP |