8UAY

Structure of Arginyl-5'-O-adenosine phosphoramidate/RNase A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	LIQUID ANODE
Source details	BRUKER METALJET
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-04-25
Detector	Bruker PHOTON II
Wavelength(s)	1.3418
Spacegroup name	C 1 2 1
Unit cell lengths	99.508, 31.128, 68.575
Unit cell angles	90.00, 91.75, 90.00

Refinement procedure

Resolution	16.580 - 1.800
R-factor	0.22996
Rwork	0.227
R-free	0.28625
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.149
Data reduction software	PROTEUM PLUS
Data scaling software	PROTEUM PLUS
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	16.760	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.112	0.487
Number of reflections	19557	2711
<I/σ(I)>	5.72	1.33
Completeness [%]	98.4	92.6
Redundancy	4	2.29

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	PROTEIN WAS CRYSTALLIZED FROM 25 percent PEG 3350, 20 MM SODIUM CITRATE, PH 5.5. Arginyl-5'-O-adenosine phosphoramidate soaking was achieved as follows. 1 uL of a stock solution of 100 mM ligand was added to 2uL of reservoir solution, to achieve a concentration of ~33 mM in the soaking solution. A few RNase A crystals were soaked for 110 - 130 minutes in the soaking solution.