Mass: 18.015 Da / Num. of mol.: 62 / Source method: isolated from a natural source / Formula: H2O
Compound details
THE AUTHORS STATE THAT THE BOUND PEPTIDE WAS CO-PURIFIED, THE SEQUENCE IS UNKNOWN, AND IT DOES NOT ...THE AUTHORS STATE THAT THE BOUND PEPTIDE WAS CO-PURIFIED, THE SEQUENCE IS UNKNOWN, AND IT DOES NOT SEEM TO CORRESPOND TO THE KKK PEPTIDE PRESENT IN THE CRYSTALLIZATION BUFFER.
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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 Å3/Da / Density % sol: 38.52 %
Crystal grow
Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1 M HEPES/Na pH 7.0, 30% jeffamine ED-2001 pH 7.0, 5mM Lys-Lys-Lys oligopeptide, cryo 30% glycerol
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Data collection
Diffraction
Mean temperature: 100 K / Serial crystal experiment: N
Resolution: 2.4→38.63 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.907 / SU B: 22.396 / SU ML: 0.242 / Cross valid method: THROUGHOUT / ESU R: 1.497 / ESU R Free: 0.312 / Stereochemistry target values: ML / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.25416
1920
9.9 %
RANDOM
Rwork
0.19456
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obs
0.20052
17407
99.91 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å