7KPP

Structure of the E102A mutant of a GNAT superfamily PA3944 acetyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2017-06-06
Detector	ADSC QUANTUM 210r
Wavelength(s)	0.979
Spacegroup name	P 1
Unit cell lengths	36.344, 44.038, 60.184
Unit cell angles	98.03, 106.88, 90.03

Refinement procedure

Resolution	43.600 - 1.450
R-factor	0.1496
Rwork	0.149
R-free	0.16840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6edd
RMSD bond length	0.004
RMSD bond angle	1.245
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.480
High resolution limit [Å]	1.450	3.940	1.450
Rmerge	0.053	0.035	0.206
Rmeas	0.052	0.040	0.240
Rpim	0.024	0.018	0.119
Number of reflections	60281	3095	2922
<I/σ(I)>	13.2
Completeness [%]	96.3	98.7	93.1
Redundancy	4.7	4.7	4
CC(1/2)		0.996	0.938

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	0.3 uL of 10 mg/mL protein incubated with 5mM CoA was mixed with 0.2 uL of the well condition (MCSG suite I condition 11 - 100 mM Tris-HCl pH 7.0, 200 mM calcium acetate, 20% w/v PEG 3000) and equilibrated against well solution in 96 Well 3 drop Crystallization Plate (Swissci).