3.1.13.4	crystal structure of the PARN-RNA-recognition motif domain (residues 445-540) with a bound 7-methylguanosine triphosphate nucleotide shows a remarkable conformational flexibility of the RNA-recognition motif domain, crystal structure is refined at a resolution of 2.1 A, protein folds into a three-stranded antiparallel beta-sheet that is flanked by one alpha-helix connecting beta-strands beta1 and beta2	
3.1.13.4	enzyme PF2046 complexed with an oligonucleotide of four thymidine nucleotides (dT4), X-ray diffraction structure determination and analysis	
3.1.13.4	free and RNA-bound forms, 20°C, hanging-drop method	
3.1.13.4	in silico model for catalytic mechanism and development of a 3D pharmacophore model. Residues Arg99 and Gln109 are involved in the regulation of catalysis. The natural preference of the enzyme for poly(A) is based on favorable biophysical electrostatic and hydrophobic interactions	
3.1.13.4	Pop2p crystallized by the sitting drop vapour diffusion technique, to 1.4 A resolution by X-ray crystallography, crystals belong to the space group P212121, contains a fully conserved DEDDh active site	
3.1.13.4	purified recombinant CNOT6L nuclease domain in complex with AMP and poly(A) DNA, hanging drop vapour diffusion method, 0.001 ml of protein solution, containing 15 mg/ml protein and 1 mM DTT, is mixed with 0.001 ml of reservoir solution and equilibrated over 300 ml reservoir solution, containing 0.1 M HEPES, pH 7.5, 1.1 M ammonium tartrate, and 0.2 M NDSB-201, at 16°C, X-ray diffraction structure determination and analysis at 1.94-2.44 A resolution	
3.1.13.4	to 2.1 A resolution, one dimer per asymmetric unit