6EBY

Crystal structure of the MbtH-like protein FscK bound to the interface forming region of FscH adenylation domain from Thermobifida fusca

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	2015-11-16
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9786
Spacegroup name	P 1 21 1
Unit cell lengths	43.450, 58.290, 58.700
Unit cell angles	90.00, 107.21, 90.00

Refinement procedure

Resolution	29.452 - 1.850
R-factor	0.2031
Rwork	0.200
R-free	0.23460
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6ea3
RMSD bond length	0.002
RMSD bond angle	0.580
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX (1.11.1_2575)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	58.290	58.290	1.890
High resolution limit [Å]	1.850	9.060	1.850
Rmerge	0.072	0.053	0.226
Rmeas	0.077	0.057	0.242
Rpim	0.028	0.022	0.087
Total number of observations	180172
Number of reflections	23530	223	1463
<I/σ(I)>	17.9
Completeness [%]	98.1	98.3	96.9
Redundancy	7.7	6.4	7.7
CC(1/2)	0.997	0.995	0.980

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	291.15	PEG 3350, sodium chloride, BisTris