9H4U

Deacetylase FI8 utilizes unconventional variant of a catalytic triad: the diluted triad

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P13 (MX1)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-04-23
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9763
Spacegroup name	P 21 21 21
Unit cell lengths	96.663, 120.040, 141.548
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.378 - 1.541
Rwork	0.170
R-free	0.20090
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.813
Data reduction software	XDS (10. Jan 2022)
Data scaling software	XDS (10. Jan 2022)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.630
High resolution limit [Å]	1.540	1.540
Rmeas	0.107	2.190
Number of reflections	2930895	274588
<I/σ(I)>	12.6	0.78
Completeness [%]	96.5	78.4
Redundancy	12.5	9
CC(1/2)	0.998	0.396

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Crystallization condition: 0.3 uL protein solution (9.3 mg/mL protein) and 0.3 uL well solution (0.2 M Ca-acetate, 0.1 M Na-cacodylate pH 6.5, 18% PEG8000). Cryo condition: 0.2 M Ca-acetate, 0.1 M Na-cacodylate, 22% PEG8000, 8% PEG400.