6MN4

Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa, H154A mutant, in complex with apramycin

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	2017-12-06
Detector	ADSC QUANTUM 210r
Wavelength(s)	0.97933
Spacegroup name	P 21 21 21
Unit cell lengths	77.550, 130.507, 264.919
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.327 - 2.800
R-factor	0.2487
Rwork	0.247
R-free	0.30430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3sma
RMSD bond length	0.005
RMSD bond angle	0.975
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	PHENIX ((dev_3092: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.850
High resolution limit [Å]	2.800	2.800
Rmerge	0.183	1.771
Rpim	0.063	0.613
Number of reflections	66374
<I/σ(I)>	12.77	1.4
Completeness [%]	95.2	97.1
Redundancy	9	8.9
CC(1/2)		0.776

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	0.1 M HEPES pH 7, 30% (w/v) PEG1k, 2.5 mM apramycin