6FL5
Structure of human SHMT1-H135N-R137A-E168N mutant at 3.6 Ang. resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-03-10 |
Detector | DECTRIS EIGER R 4M |
Wavelength(s) | 0.96770 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 139.719, 139.719, 267.377 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.010 - 3.600 |
R-factor | 0.263 |
Rwork | 0.262 |
R-free | 0.27710 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bj4 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.638 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.32) |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 56.610 | 56.610 | 3.790 |
High resolution limit [Å] | 3.600 | 11.380 | 3.600 |
Rmerge | 0.312 | 0.075 | 1.019 |
Rmeas | 0.340 | 0.082 | 1.107 |
Rpim | 0.131 | 0.033 | 0.425 |
Number of reflections | 30938 | 1139 | 4471 |
<I/σ(I)> | 5.6 | ||
Completeness [%] | 98.2 | 98.6 | 99.2 |
Redundancy | 6.3 | 5.6 | 6.5 |
CC(1/2) | 0.973 | 0.996 | 0.570 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | 2 microL of 80microM protein solution in: 20 mM Hepes pH7.2, 250 mM NaCl 5% glycerol + 2 microL of reservoir:0.1 M Na Cacodilate pH6.5 - 1M Na citrate |