ANALYTICAL SIZE-EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A MONOMER AS THE SIGNIFICANT OLIGOMERIC FORM IN SOLUTION.
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Components
#1: Protein
hypotheticalproteinBT_3535 / Hypothesis
Mass: 24645.857 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacteroides thetaiotaomicron VPI-5482 (bacteria) Gene: BT_3535 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): HK100 / References: UniProt: Q8A1X3
Sequence details
THE CONSTRUCT (RESIDUES 18-234) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 18-234) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
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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: 4 Å3/Da / Density % sol: 69.23 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.93 Details: 40.9000% 2-methyl-2,4-pentanediol, 0.1M HEPES pH 6.93, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Monochromator: Single crystal Si(111) bent monochromator (horizontal focusing) Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.91162
1
2
0.97941
1
Reflection
Resolution: 2.6→28.831 Å / Num. obs: 12900 / % possible obs: 99.9 % / Redundancy: 10.5 % / Rmerge(I) obs: 0.124 / Rsym value: 0.124 / Net I/σ(I): 16.7
Reflection shell
Rmerge(I) obs: 0.011 / Diffraction-ID: 1
Resolution (Å)
Redundancy (%)
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
2.6-2.67
10.7
0.7
10029
941
1.056
100
2.67-2.74
10.8
0.9
9701
902
0.822
100
2.74-2.82
10.8
1.1
9399
870
0.692
100
2.82-2.91
10.8
1.4
9369
866
0.564
100
2.91-3
10.7
1.8
9033
842
0.44
100
3-3.11
10.8
2.4
8566
790
0.326
100
3.11-3.22
10.7
3
8399
784
0.259
100
3.22-3.36
10.6
3.8
8120
763
0.199
100
3.36-3.51
10.7
4.7
7630
715
0.154
100
3.51-3.68
10.7
5.8
7463
700
0.125
100
3.68-3.88
10.5
6.7
7087
672
0.109
100
3.88-4.11
10.6
7.7
6580
621
0.094
100
4.11-4.39
10.5
9.1
6332
604
0.074
100
4.39-4.75
10.4
10.8
5902
567
0.063
100
4.75-5.2
10.4
10.8
5322
513
0.061
100
5.2-5.81
10.3
9.6
4904
478
0.07
100
5.81-6.71
10
9.2
4280
429
0.073
100
6.71-8.22
9.8
10.1
3576
364
0.063
100
8.22-11.63
9.3
10.9
2841
304
0.053
100
11.63-28.83
8
12.4
1398
175
0.048
93.8
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
REFMAC
5.5.0053
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
SCALA
3.2.5
datascaling
PDB_EXTRACT
3.006
dataextraction
MOSFLM
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2.6→28.831 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.922 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 18.125 / SU ML: 0.171 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.269 / ESU R Free: 0.224 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.239
629
4.9 %
RANDOM
Rwork
0.202
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-
-
obs
0.204
12878
99.87 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
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