Mass: 18.015 Da / Num. of mol.: 247 / 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: 2.93 Å3/Da / Density % sol: 57.98 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 9 Details: 1.6000M (NH4)2SO4, 0.1M Bicine pH 9.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution: 1.62→29.348 Å / Num. obs: 45318 / % possible obs: 100 % / Redundancy: 9.6 % / Rmerge(I) obs: 0.075 / Rsym value: 0.075 / Net I/σ(I): 19.8
Reflection shell
Diffraction-ID: 1
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.62-1.66
7.4
0.684
2.2
23949
3245
0.684
99.6
1.66-1.71
7.4
0.535
2.9
23767
3219
0.535
100
1.71-1.76
7.4
0.421
3.7
23246
3145
0.421
100
1.76-1.81
7.4
0.33
4.8
22491
3033
0.33
100
1.81-1.87
7.4
0.264
6.2
21906
2958
0.264
100
1.87-1.94
7.4
0.21
8.1
21462
2885
0.21
100
1.94-2.01
7.4
0.173
10.3
20440
2760
0.173
100
2.01-2.09
7.4
0.136
14
19845
2677
0.136
100
2.09-2.18
7.4
0.11
18.9
18911
2551
0.11
100
2.18-2.29
7.4
0.096
21.5
18148
2447
0.096
100
2.29-2.41
10.7
0.114
24.9
25273
2370
0.114
100
2.41-2.56
12.1
0.108
28.1
27025
2228
0.108
100
2.56-2.74
14.4
0.101
33.1
29895
2073
0.101
100
2.74-2.96
14.6
0.09
37.4
28643
1962
0.09
100
2.96-3.24
14.5
0.075
44.1
26174
1803
0.075
100
3.24-3.62
14.5
0.066
49
23812
1645
0.066
100
3.62-4.18
14.3
0.059
52.7
21118
1476
0.059
100
4.18-5.12
14
0.06
52.1
17659
1259
0.06
100
5.12-7.24
13.8
0.061
49.9
13622
990
0.061
100
7.24-29.36
12.2
0.052
50.1
7203
592
0.052
98.5
-
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: 1.62→29.348 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.958 / Occupancy max: 1 / Occupancy min: 0.2 / SU B: 3.386 / SU ML: 0.053 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.082 / ESU R Free: 0.079 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY OTHER REFINEMENT REMARKS: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORD CONTAINS RESIDUAL B ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY OTHER REFINEMENT REMARKS: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3.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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4.GLYCEROL MOLECULE USED AS CRYOPROTECTANT IS MODELED IN THE STRUCTURE.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.201
2280
5 %
RANDOM
Rwork
0.182
-
-
-
obs
0.183
45270
99.95 %
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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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