8HQR

Crystal structure of the arginine-/lysine-binding protein SAR11_1210 from 'Candidatus Pelagibacter ubique' HTCC1062 bound to arginine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL32XU
Synchrotron site	SPring-8
Beamline	BL32XU
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-07-28
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	57.128, 84.689, 106.097
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.400 - 1.320
R-factor	0.15094
Rwork	0.149
R-free	0.19047
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5ot8
RMSD bond length	0.009
RMSD bond angle	1.525
Data reduction software	XDS (Jan 10, 2022)
Data scaling software	XDS (Jan 10, 2022)
Phasing software	MOLREP (11.9.02)
Refinement software	REFMAC (5.8.0352)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.400	1.400
High resolution limit [Å]	1.320	1.320
Rmerge	0.123	1.411
Rmeas	0.129	1.476
Number of reflections	121098	19320
<I/σ(I)>	10.44	1.16
Completeness [%]	99.4	99.1
Redundancy	12.2	11.6
CC(1/2)	0.996	0.709

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	293	1 uL 12 mg/mL protein + 1 uL 21% (w/v) PEG 1500, 0.1 M MES pH 6.0. Final crystal obtained by serial microseeding from this condition. Crystal cryoprotected in 30% (w/v) PEG 1500, 0.1 M MES pH 6.0.