ANAPHASE-PROMOTINGCOMPLEXSUBUNIT8 / 20S CYCLOSOME/APC COMPLEX PROTEIN APC8 / CELL UNTIMELY TORN PROTEIN 23 / 20S CYCLOSOME/APC COMPLEX ...20S CYCLOSOME/APC COMPLEX PROTEIN APC8 / CELL UNTIMELY TORN PROTEIN 23 / 20S CYCLOSOME/APC COMPLEX PROTEIN APC8 / CELL UNTIMELY TORN PROTEIN 23
Mass: 33869.430 Da / Num. of mol.: 2 / Fragment: N-TERM, UNP RESIDUES 19-301 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SCHIZOSACCHAROMYCES POMBE (fission yeast) Description: SOURCE DETAILS ARE THE SAME AS 3ZN3 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O94556
Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 2.69 Å / Relative weight: 1
Reflection
Resolution: 3.1→61.25 Å / Num. obs: 282255 / % possible obs: 99.7 % / Observed criterion σ(I): 4.8 / Redundancy: 27.8 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 30.1
Reflection shell
Resolution: 3.1→3.21 Å / Redundancy: 17.8 % / Rmerge(I) obs: 0.72 / Mean I/σ(I) obs: 4.8 / % possible all: 98
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0135
refinement
XDS
datareduction
SCALA
datascaling
SHELXD
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 3.1→61.25 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.865 / SU B: 21.509 / SU ML: 0.378 / Cross valid method: THROUGHOUT / ESU R Free: 0.519 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.25963
510
5 %
RANDOM
Rwork
0.18689
-
-
-
obs
0.19046
9615
99.73 %
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Solvent computation
Ion probe radii: 0.9 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: MASK