LYSINE-SPECIFICDEMETHYLASE6B / JMJD3 / JMJC DOMAIN-CONTAINING PROTEIN 3 / JUMONJI DOMAIN-CONTAINING PROTEIN 3 / LYSINE DEMETHYLASE 6B
Mass: 37686.949 Da / Num. of mol.: 2 / Fragment: JUMONJI DOMAIN, RESIDUES 1173-1502 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC28-BSA4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)-R3-PRARE2 References: UniProt: O15054, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
Monochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9795 Å / Relative weight: 1
Reflection
Resolution: 1.8→29.16 Å / Num. obs: 61104 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 4.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 8.5
Reflection shell
Resolution: 1.8→1.9 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.96 / Mean I/σ(I) obs: 2 / % possible all: 100
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Processing
Software
Name
Version
Classification
REFMAC
5.5.0110
refinement
MOSFLM
datareduction
SCALA
datascaling
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 1.8→29.16 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.953 / SU B: 5.236 / SU ML: 0.079 / Cross valid method: THROUGHOUT / ESU R: 0.103 / ESU R Free: 0.102 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.21578
3016
5 %
RANDOM
Rwork
0.18324
-
-
-
obs
0.18486
61100
99.74 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK