8UB1

Structure of Butyl-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	2023-01-30
Detector	Bruker PHOTON II
Wavelength(s)	1.3418
Spacegroup name	C 1 2 1
Unit cell lengths	100.027, 32.123, 72.425
Unit cell angles	90.00, 90.71, 90.00

Refinement procedure

Resolution	19.570 - 1.530
R-factor	0.24773
Rwork	0.245
R-free	0.29675
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.489
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]	19.570	1.630
High resolution limit [Å]	1.530	1.530
Rmerge	0.089	0.601
Number of reflections	35060	5972
<I/σ(I)>	11.74	1.1
Completeness [%]	99.5	99.4
Redundancy	8.2	3.88

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	25% PEG 3350, 20 MM SODIUM CITRATE PROTEIN WAS CRYSTALLIZED FROM 25% PEG 3350, 20 MM SODIUM CITRATE, PH 5.5 Butyl-5'-O-adenosine phosphoramidate was soaked into the crystals using a stock solution of 100 mM, to achieve ~35 mM in the soaking solution.