6GGV

Structure of the arginine-bound form of truncated (residues 20-233) ArgBP from T. maritima

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2011-09-20
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.5418
Spacegroup name	P 21 2 21
Unit cell lengths	30.700, 52.139, 221.343
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.690
R-factor	0.17723
Rwork	0.175
R-free	0.22599
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4psh
RMSD bond length	0.014
RMSD bond angle	1.503
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.640
High resolution limit [Å]	2.600	2.600
Rmerge	0.084
Number of reflections	9570
<I/σ(I)>	20.7
Completeness [%]	85.6
Redundancy	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	The crystals were obtained using a protein concentration of 16 mg/mL and in 0.1 M Cadmium chloride hydrate, 0.1 M Sodium acetate trihydrate (pH 4.6), 30% (v/v) Polyethylene glycol 400. Crystal quality was enhanced in presence of 2.0 M Sodium Thiocyanate or 1.0 M Sodium Bromide.