7L0A

Crystal structure of s-formylglutathione hydrolase (FrmB) from Staphylococcus aureus, apoenzyme

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-02-28
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97918
Spacegroup name	C 1 2 1
Unit cell lengths	128.303, 80.500, 66.651
Unit cell angles	90.00, 113.84, 90.00

Refinement procedure

Resolution	36.810 - 1.600
R-factor	0.158
Rwork	0.157
R-free	0.17700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4rgy
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	1.630
High resolution limit [Å]	1.600	1.600
Rmerge	0.075	0.415
Rmeas	0.093	0.059
Rpim	0.054	0.034
Total number of observations	217757
Number of reflections	78193	3961
<I/σ(I)>	11.7
Completeness [%]	96.4	99.1
Redundancy	2.8	2.8
CC(1/2)		0.992

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.7	289	20 uL hanging drops containing a 1:1 mixture of protein (6 mg/mL) and crystallization buffer (0.1 M Tricine pH 7.7, 15% PEG6K, 2.5 M NaCl, 0.125% n-dodecyl-B-D-glucoside)