response to methotrexate / dihydrofolate reductase / dihydrofolate reductase activity / tetrahydrofolate biosynthetic process / one-carbon metabolic process / response to xenobiotic stimulus / response to antibiotic Similarity search - Function
Dihydrofolate reductase, type II / R67 dihydrofolate reductase / SH3 type barrels. - #60 / Mechanosensitive ion channel MscS, beta-domain superfamily / Electron transport accessory-like domain superfamily / SH3 type barrels. / Roll / Mainly Beta Similarity search - Domain/homology
Mass: 18.015 Da / Num. of mol.: 64 / 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: 2.22 Å3/Da / Density % sol: 44.66 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: The protein was concentrated to 20 mg/mL in 100 mM Tris pH 8.0. Immediately before crystallization, chymotrypsin was added to the sample in a ratio of 1:100 chymotrypsin:protein, and the ...Details: The protein was concentrated to 20 mg/mL in 100 mM Tris pH 8.0. Immediately before crystallization, chymotrypsin was added to the sample in a ratio of 1:100 chymotrypsin:protein, and the protein was diluted to 15 mg/mL using MPD, resulting in a final MPD concentration of 25%. Reservoirs were prepared using 750 uL of 100 mM sodium phosphate pH 7.6 and 60% MPD in a Greiner 24-well hanging-drop crystallization plate. On a siliconized glass cover slip (Hampton Research), 1.5 uL of protein were combined with 2.5 uL of reservoir solution and suspended over the well. The plate was incubated at 277 K and crystals were obtained in a few days.
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Data collection
Diffraction
Mean temperature: 93 K / Serial crystal experiment: N
Resolution: 1.4→41.09 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.975 / SU B: 0.725 / SU ML: 0.029 / SU R Cruickshank DPI: 0.0493 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.049 / ESU R Free: 0.049 Details: Authors state that inhibitor LBA is partially modelled at the active site. Binding of the ligand has been confirmed biochemically, and ligand disorder outside of the pore center has been ...Details: Authors state that inhibitor LBA is partially modelled at the active site. Binding of the ligand has been confirmed biochemically, and ligand disorder outside of the pore center has been observed for other known ligands. More details can be found in the primary citation.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1577
624
5.1 %
RANDOM
Rwork
0.1412
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obs
0.142
11543
99.62 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
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