CELLDIVISIONPROTEINZAPC / FTSZ-ASSOCIATED PROTEIN C / Z-RING-ASSOCIATED PROTEIN C
Mass: 21080.717 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P75862
Has protein modification
Y
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION
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Sample preparation
Crystal
Density Matthews: 2.68 Å3/Da / Density % sol: 56.6 % / Description: NONE
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97858 Å / Relative weight: 1
Reflection
Resolution: 2.9→50 Å / Num. obs: 10807 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 41.8 % / Rmerge(I) obs: 0.3 / Net I/σ(I): 17
Reflection shell
Resolution: 2.9→3.06 Å / Redundancy: 40.7 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 3.9 / % possible all: 100
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0131
refinement
XDS
datareduction
SCALA
datascaling
PHASER
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 2.9→50.01 Å / Cor.coef. Fo:Fc: 0.912 / Cor.coef. Fo:Fc free: 0.893 / SU B: 33.423 / SU ML: 0.256 / Cross valid method: THROUGHOUT / ESU R Free: 0.377 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24734
508
4.8 %
RANDOM
Rwork
0.21306
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-
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obs
0.21474
10114
99.48 %
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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