Mass: 24155.350 Da / Num. of mol.: 2 / Source method: obtained synthetically Details: RNA was prepared by in vitro transcription with T7 RNA Polymerase in Thermotoga maritima
#2: Protein
polyApolymerase / A-adding enzyme
Mass: 45721.840 Da / Num. of mol.: 2 / Fragment: residues 1-390 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus (bacteria) / Plasmid: pET / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: O66728, polynucleotide adenylyltransferase
Resolution: 2.8→2.87 Å / Mean I/σ(I) obs: 4.3 / Rsym value: 0.398 / % possible all: 95.7
-
Processing
Software
Name
Classification
HKL-2000
datacollection
SCALEPACK
datascaling
MLPHARE
phasing
CNS
refinement
HKL-2000
datareduction
Refinement
Method to determine structure: MAD / Resolution: 2.8→40 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: This crystal has a pseudo-merohedral perfect twinning in P2, which pretends P2(1)2(1)2. beta is 90 degree since Depositors processed the data with P2(1)2(1)2, and expanded them to the P2 ...Details: This crystal has a pseudo-merohedral perfect twinning in P2, which pretends P2(1)2(1)2. beta is 90 degree since Depositors processed the data with P2(1)2(1)2, and expanded them to the P2 space group. The file contains Friedel pairs.
Rfactor
Num. reflection
Selection details
Rfree
0.2865
1945
RANDOM
Rwork
0.2297
-
-
all
-
39038
-
obs
-
39038
-
Displacement parameters
Biso mean: 87.8 Å2
Refine analyze
Free
Obs
Luzzati coordinate error
0.41 Å
0.36 Å
Luzzati d res low
-
5 Å
Luzzati sigma a
0.55 Å
0.42 Å
Refinement step
Cycle: LAST / Resolution: 2.8→40 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
5794
1384
62
79
7319
Refine LS restraints
Refine-ID
Type
Dev ideal
X-RAY DIFFRACTION
c_bond_d
0.012
X-RAY DIFFRACTION
c_angle_deg
1.52
X-RAY DIFFRACTION
c_dihedral_angle_d
22.1
X-RAY DIFFRACTION
c_improper_angle_d
1.23
LS refinement shell
Resolution: 2.8→2.9 Å
Rfactor
Num. reflection
% reflection
Rfree
0.3263
180
-
Rwork
0.3013
-
-
obs
-
-
95 %
+
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