8UAX

Structure of Alanyl-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	2023-01-31
Detector	Bruker PHOTON II
Wavelength(s)	1.3418
Spacegroup name	C 1 2 1
Unit cell lengths	100.228, 32.373, 72.639
Unit cell angles	90.00, 90.32, 90.00

Refinement procedure

Resolution	19.620 - 1.900
R-factor	0.22055
Rwork	0.218
R-free	0.27317
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.641
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]	19.620	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.123	0.481
Number of reflections	18628	2613
<I/σ(I)>	7.78	2.08
Completeness [%]	99.2	99.2
Redundancy	6.1	4.17

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. Alanyl-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 ~35mM in the soaking solution. A few RNase A crystals were soaked for 120 - 130 minutes in the soaking solution.