Mass: 18.015 Da / Num. of mol.: 280 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.66 Å3/Da / Density % sol: 53.71 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 0.2000M NaFormate, 20.0000% PEG-3350, No Buffer pH 7.2, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution: 2.25→32.126 Å / Num. obs: 26590 / % possible obs: 97.9 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.068 / Net I/σ(I): 9.39
Reflection shell
Resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
Diffraction-ID
% possible all
2.25-2.31
0.491
1.5
6395
3372
1
89.6
2.31-2.37
0.398
1.9
6819
3551
1
98.6
2.37-2.44
0.322
2.3
6794
3544
1
99.1
2.44-2.51
0.29
2.6
6502
3386
1
98.9
2.51-2.6
0.233
3.1
6353
3295
1
98.9
2.6-2.69
0.234
3.3
6140
3185
1
99.1
2.69-2.79
0.17
4.2
5990
3120
1
99
2.79-2.9
0.146
5.2
5703
2947
1
99.1
2.9-3.03
0.111
6.6
5501
2850
1
99.1
3.03-3.18
0.091
7.8
5185
2702
1
99
3.18-3.35
0.071
10.3
5053
2620
1
99.4
3.35-3.56
0.05
13.8
4638
2415
1
98.2
3.56-3.8
0.039
17.4
4439
2301
1
98.3
3.8-4.11
0.032
20.6
4116
2121
1
98.4
4.11-4.5
0.031
22.7
3816
1940
1
98.3
4.5-5.03
0.026
23.9
3356
1731
1
97.2
5.03-5.81
0.029
22.3
3082
1572
1
97.6
5.81-7.11
0.028
23.8
2520
1279
1
96.7
7.11-10.06
0.019
30.8
1998
1008
1
96.7
10.06-32.126
0.017
38.1
1048
528
1
93
-
Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
REFMAC
5.5.0109
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
XSCALE
datascaling
PDB_EXTRACT
3.006
dataextraction
XDS
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2.25→32.126 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.934 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 13.9 / SU ML: 0.149 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.269 / ESU R Free: 0.204 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. 4. FORMATE (FMT) AND ETHYLENE GLYCOL (EDO) MODELED WERE PRESENT IN CRYSTALLIZATION OR CRYO CONDITIONS. 5. REGIONS OF POOR ELECTRON DENSITY:20-28,113-121, 197-203,226-236. MODEL AT THOSE REGIONS IS NOT RELIABLE.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.227
1339
5 %
RANDOM
Rwork
0.185
-
-
-
obs
0.187
26590
99.23 %
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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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