Mass: 18.015 Da / Num. of mol.: 746 / Source method: isolated from a natural source / Formula: H2O
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Details
Compound details
ENGINEERED RESIDUE IN CHAIN A, ASP 214 TO ALA ENGINEERED RESIDUE IN CHAIN B, ASP 214 TO ALA
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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: 2.7 Å3/Da / Density % sol: 55 % Description: SINCE THE UNIT-CELL PARAMETERS FOR D214A TPL CRYSTAL WERE ONLY SLIGHTLY DIFFERENT THAN FOR THE NATIVE HOLOENZYME, IT WAS POSSIBLE TO REFINE THE D214A TPL MUTANT STRUCTURE IN REFMAC USING ...Description: SINCE THE UNIT-CELL PARAMETERS FOR D214A TPL CRYSTAL WERE ONLY SLIGHTLY DIFFERENT THAN FOR THE NATIVE HOLOENZYME, IT WAS POSSIBLE TO REFINE THE D214A TPL MUTANT STRUCTURE IN REFMAC USING THE WILD-TYPE TPL HOLOENZYME STRUCTURE, PDB ENTRY 2EZ1, AS A STARTING MODEL.
Crystal grow
Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: THE CRYSTALS WERE GROWN AT 293 K BY THE HANGING DROP VAPOR DIFFUSION TECHNIQUE BY MIXING 2 UL OF THE PROTEIN SOLUTION, 18-20 MG/ML, WITH AN EQUAL VOLUME OF THE RESERVOIR SOLUTION CONTAINING ...Details: THE CRYSTALS WERE GROWN AT 293 K BY THE HANGING DROP VAPOR DIFFUSION TECHNIQUE BY MIXING 2 UL OF THE PROTEIN SOLUTION, 18-20 MG/ML, WITH AN EQUAL VOLUME OF THE RESERVOIR SOLUTION CONTAINING 50 MMOL/L TRIETHANOLAMINE BUFFER PH 8.0, 0.4-0.8 MOL/L KCL, 0.35-0.38 G/ML PEG 5000 MME, 5 MMOL/L PYRIDOXAL-5-PHOSPHATE, AND 2 MMOL/L DITHIOTHREITOL.
Resolution: 1.91→25 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.967 / SU B: 5.454 / SU ML: 0.075 / Cross valid method: THROUGHOUT / ESU R: 0.118 / ESU R Free: 0.106 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.17711
1283
1.5 %
RANDOM
Rwork
0.15571
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obs
0.15604
85457
98.56 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK