Mass: 18.015 Da / Num. of mol.: 646 / Source method: isolated from a natural source / Formula: H2O
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.34 Å3/Da / Density % sol: 47.47 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, hanging drop Details: THE PURIFIED PROTEIN WAS DISSOLVED IN 50 MM TRIS-HCL, PH 7.5 AND CONCENTRATED TO 11 MG/ML. 1 UL OF PROTEIN SOLUTION WAS EQUILIBRATED AGAINST 1 UL OF RESERVOIR SOLUTION CONTAINING 16-20% ...Details: THE PURIFIED PROTEIN WAS DISSOLVED IN 50 MM TRIS-HCL, PH 7.5 AND CONCENTRATED TO 11 MG/ML. 1 UL OF PROTEIN SOLUTION WAS EQUILIBRATED AGAINST 1 UL OF RESERVOIR SOLUTION CONTAINING 16-20% PEG3350, 100 MM MES PH 5.5 AND 50 MM ZNACETATE
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.934 Å / Relative weight: 1
Reflection
Resolution: 1.83→82.53 Å / Num. obs: 29051 / % possible obs: 98.1 % / Observed criterion σ(F): -3 / Redundancy: 11 % / Biso Wilson estimate: 19 Å2 / Rmerge(I) obs: 0.102 / Net I/σ(I): 20.89
Reflection shell
Resolution: 1.83→1.89 Å / Redundancy: 11.2 % / Rmerge(I) obs: 0.467 / Mean I/σ(I) obs: 5.81 / % possible all: 97.5
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Processing
Software
Name
Version
Classification
REFMAC
5.2.0019
refinement
XDS
datareduction
XSCALE
datascaling
REFMAC
5.2.0019
phasing
Refinement
Resolution: 1.83→62.38 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.938 / SU B: 2.272 / SU ML: 0.072 / Cross valid method: THROUGHOUT / ESU R: 0.123 / ESU R Free: 0.128 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.19922
1999
6.9 %
RANDOM
Rwork
0.14093
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obs
0.14495
27051
98.13 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å