6S0M

Structural and dynamic studies provide insights into specificity and allosteric regulation of Ribonuclease AS, a key enzyme in mycobacterial virulence

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	Cu FINE FOCUS
Temperature [K]	100
Detector technology	CCD
Collection date	2018-10-10
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54
Spacegroup name	P 21 21 21
Unit cell lengths	42.464, 77.068, 104.572
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.000
R-factor	0.18104
Rwork	0.178
R-free	0.24161
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.024
RMSD bond angle	1.950
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]	30.000	2.030
High resolution limit [Å]	2.000	2.000
Number of reflections	23972	1170
<I/σ(I)>	20.2
Completeness [%]	99.9
Redundancy	6.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION		277	protein concentration of 14 mg/mL in 0.1M HEPES pH 7.5, 10% w/v polyethylene glycol 8,000, 8% v/v ethylene glycol. Crystals of the complex of RNase AS with GMP were prepared by soaking crystals of native protein in a solution containing GMP at 20 mM.