7K47
Crystal Structure of Glucosamine-1-phosphate N-acetyltransferase from Stenotrophomonas maltophilia K279a
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 | CCD |
Collection date | 2020-07-16 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97856 |
Spacegroup name | P 63 |
Unit cell lengths | 91.290, 91.290, 184.550 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.880 - 2.900 |
R-factor | 0.1774 |
Rwork | 0.174 |
R-free | 0.20540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | two domains of PDB entry 5vmk as per Morda |
RMSD bond length | 0.004 |
RMSD bond angle | 0.610 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MoRDa |
Refinement software | PHENIX (1.18.2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.980 |
High resolution limit [Å] | 2.900 | 12.970 | 2.900 |
Rmerge | 0.051 | 0.037 | 0.543 |
Rmeas | 0.054 | 0.040 | 0.568 |
Number of reflections | 19333 | 223 | 1433 |
<I/σ(I)> | 30.57 | 52.9 | 4.83 |
Completeness [%] | 99.9 | 95.7 | 100 |
Redundancy | 11.482 | 8.91 | 11.585 |
CC(1/2) | 1.000 | 0.999 | 0.947 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 287 | Optimization screen based on Rigaku Reagens JCSG+ condition B4: 100mM HEPES free acid / Sodium hydroxide pH 8.0, 8% (V/V) ethylene glycol, 9.6% (w/V) PEG 8000: StmaA.00150.a.B1.PW38698 at 24mg/ml: tray 319930h10: cryo: 20% EG in 2 steps: puck aod1-6 |