A: 3-ketoacyl-CoA thiolase-like protein B: 3-ketoacyl-CoA thiolase-like protein C: 3-ketoacyl-CoA thiolase-like protein D: 3-ketoacyl-CoA thiolase-like protein hetero molecules
Component-ID: _ / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: ILE / End label comp-ID: ILE / Refine code: _ / Auth seq-ID: 12 - 441 / Label seq-ID: 28 - 457
Dom-ID
Ens-ID
Auth asym-ID
Label asym-ID
1
1
A
A
2
1
B
B
1
2
A
A
2
2
C
C
1
3
A
A
2
3
D
D
1
4
B
B
2
4
C
C
1
5
B
B
2
5
D
D
1
6
C
C
2
6
D
D
NCS ensembles :
ID
1
2
3
4
5
6
-
Components
#1: Protein
3-ketoacyl-CoAthiolase-likeprotein
Mass: 49225.926 Da / Num. of mol.: 4 / Mutation: C123A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Leishmania mexicana (eukaryote) / Gene: LMXM_23_0690 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: E9AW84, acetyl-CoA C-acyltransferase
Mass: 18.015 Da / Num. of mol.: 830 / 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: 2.1 Å3/Da / Density % sol: 41.5 %
Crystal grow
Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 100 mM Bis Tris propane, pH 7.5, 0.2M sodium fluoride and 20% w/v PEG 3350
Resolution: 1.98→119.63 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.913 / SU B: 5.012 / SU ML: 0.137 / Cross valid method: THROUGHOUT / ESU R: 0.209 / ESU R Free: 0.168 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.22607
5300
4.9 %
RANDOM
Rwork
0.18934
-
-
-
obs
0.19113
103007
99.14 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å