9CE6
Key structural role for the conserved cis-proline of soybean serine hydroxymethyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 293 |
Detector technology | CMOS |
Collection date | 2024-04-04 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 116.603, 129.685, 58.629 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.340 - 2.250 |
R-factor | 0.1946 |
Rwork | 0.191 |
R-free | 0.25630 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.938 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.570 | 2.320 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.080 | 2.437 |
Rpim | 0.044 | 1.354 |
Number of reflections | 43034 | 3891 |
<I/σ(I)> | 13.5 | 0.9 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.9 | 8.1 |
CC(1/2) | 0.999 | 0.537 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M Hepes, pH 7.5 20% w/v PEG 3350 2% v/v tacsimate, pH 7.0 |