VACUOLARMEMBRANEPROTEINPEP3 / CARBOXYPEPTIDASE Y-DEFICIENT PROTEIN 3 / VACUOLAR MORPHOGENESIS PROTEIN 8 / VACUOLAR PROTEIN ...CARBOXYPEPTIDASE Y-DEFICIENT PROTEIN 3 / VACUOLAR MORPHOGENESIS PROTEIN 8 / VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 / VACUOLAR PROTEIN-TARGETING PROTEIN 18 / VPS18
Mass: 40405.297 Da / Num. of mol.: 2 / Fragment: BETA-PROPELLER, RESIDUES 2-348 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PQLINKH / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA2 / References: UniProt: P27801
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.91841 Å / Relative weight: 1
Reflection
Resolution: 2.14→63.12 Å / Num. obs: 39106 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 27 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 11.3
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0073
refinement
XDS
datareduction
Refinement
Method to determine structure: OTHER Starting model: NONE Resolution: 2.14→43.31 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.913 / SU B: 12.945 / SU ML: 0.169 / Cross valid method: THROUGHOUT / ESU R: 0.276 / ESU R Free: 0.21 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS WITH TLS ADDED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24445
2648
6.8 %
RANDOM
Rwork
0.20138
-
-
-
obs
0.20431
36420
98.77 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK