7KPS

Structure of a GNAT superfamily PA3944 acetyltransferase in complex with AcCoA

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	2017-03-09
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.979
Spacegroup name	P 1
Unit cell lengths	36.563, 44.246, 60.183
Unit cell angles	97.94, 106.72, 89.92

Refinement procedure

Resolution	37.430 - 1.800
R-factor	0.2078
Rwork	0.206
R-free	0.23540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6edd
RMSD bond length	0.003
RMSD bond angle	1.180
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	1.830
High resolution limit [Å]	1.800	4.880	1.800
Rmerge	0.095	0.027	0.592
Rmeas	0.102	0.035	0.809
Rpim	0.068	0.023	0.549
Number of reflections	32365	1659	1609
<I/σ(I)>	5.5
Completeness [%]	97.1	98.9	95.6
Redundancy	2.2	2.2	1.9
CC(1/2)		0.985	0.553

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 AcCoA and 5 mM (R)-3-(2-chloroacetamido)-4-(((S)-1-methoxy-1-oxo-3-phenylpropan-2-yl)amino)-4-oxobutanoic acid 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).