6XHE

Structure of beta-prolinyl 5'-O-adenosine phosphoramidate

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	2019-07-10
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	101.002, 32.795, 74.090
Unit cell angles	90.00, 90.33, 90.00

Refinement procedure

Resolution	29.810 - 1.880
R-factor	0.20769
Rwork	0.205
R-free	0.26463
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Single RNase molecule from PDB-ID
RMSD bond length	0.007
RMSD bond angle	1.578
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.810	1.970
High resolution limit [Å]	1.880	1.880
Rmerge	0.094	0.951
Number of reflections	19587	1765
<I/σ(I)>	24.93
Completeness [%]	98.2	89.5
Redundancy	7.1	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	PROTEIN WAS CRYSTALLIZED FROM 25% PEG 3350, 20 MM SODIUM CITRATE, PH 5.5, Glycinyl-5'-O-adenosine phosphoramidate soaking was achieved as follows. 1 uL of a stock solution of 50 mM ligand was added to 2uL of reservoir solution, to achieve a concentration of ~25 mM in the soaking solution. A few RNase A crystals were soaked for 45 - 90 minutes in the soaking solution