7OVG

The C146A variant of an amidase from Pyrococcus horikoshii with bound acetamide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	170
Detector technology	PIXEL
Collection date	2019-09-20
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.9763
Spacegroup name	P 1
Unit cell lengths	44.979, 57.012, 61.358
Unit cell angles	68.09, 85.16, 76.93

Refinement procedure

Resolution	43.850 - 1.650
R-factor	0.1527
Rwork	0.151
R-free	0.18204
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6ypa
RMSD bond length	0.014
RMSD bond angle	1.626
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHENIX
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.860	1.709
High resolution limit [Å]	1.650	1.650
Rmerge	0.056	0.367
Rmeas	0.065	0.444
Rpim	0.035	0.246
Number of reflections	53852	2008
<I/σ(I)>	11.32	2.39
Completeness [%]	81.1	30.28
Redundancy	3.4	3
CC(1/2)	0.996	0.927

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The crystallization condition is: 5mg/mL protein, 0.1M potassium chloride, 0.2M Sodium formate; 0.2M Ammonium acetate; 0.2M Sodium citrate tribasic dihydrate; 0.2M Sodium potassium tartrate tetrahydrate; 0.1M acetamide; Imidazole; MES monohydrate (acid); 25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350