7U6M
Albumin binding domain fused to a mutant of the Erwinia asparaginase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-06-29 |
| Detector | DECTRIS EIGER R 1M |
| Wavelength(s) | 1.1272 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 80.150, 130.410, 155.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.980 - 1.750 |
| R-factor | 0.1454 |
| Rwork | 0.144 |
| R-free | 0.16560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5i48 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.653 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.800 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Number of reflections | 163730 | 25735 |
| <I/σ(I)> | 8.62 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 15.8 | |
| CC(1/2) | 0.996 | 0.800 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 294 | ABD-ErA-(TM) at 5 mg/ml in the presence of 5 mM aspartate was crystallized using the hanging drop method at room temperature in 12-17% PEG 3350, 0.1 ammonium citrate, pH 7.0, by mixing 2 microliters of protein with 1 microliter of reservoir solution |
