8DTC
Crystal Structure of Glucokinase with bound glucose from Acanthamoeba castellanii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2021-04-01 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.9787 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 114.990, 52.790, 118.350 |
Unit cell angles | 90.00, 118.62, 90.00 |
Refinement procedure
Resolution | 39.380 - 2.250 |
R-factor | 0.1705 |
Rwork | 0.169 |
R-free | 0.20130 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | AlphaFold2 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1-4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.380 | 39.380 | 2.310 |
High resolution limit [Å] | 2.250 | 10.060 | 2.250 |
Rmerge | 0.080 | 0.030 | 0.522 |
Rmeas | 0.093 | 0.035 | 0.618 |
Total number of observations | 222043 | ||
Number of reflections | 59214 | 676 | 4410 |
<I/σ(I)> | 12.35 | 34.15 | 2.29 |
Completeness [%] | 98.7 | 90.5 | 99.5 |
Redundancy | 3.75 | 3.506 | 3.395 |
CC(1/2) | 0.997 | 0.998 | 0.737 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 287 | AccaA.19900.a.Q2.PS38640 at 25.33 mg/mL was mixed 1:1 (0.2 uL protein and 0.2 uL precipitant) with 0.1 M MES: NaOH, pH 6.5, 1.6 M Magnesium Sulfate (MCSG-1 E5). [Barcode: 321398e5] [pin: bzu2-8] [cryo: 20% Ethylene glycol] |