A: Hypothetical nigD-like protein B: Hypothetical nigD-like protein C: Hypothetical nigD-like protein D: Hypothetical nigD-like protein E: Hypothetical nigD-like protein F: Hypothetical nigD-like protein G: Hypothetical nigD-like protein H: Hypothetical nigD-like protein I: Hypothetical nigD-like protein J: Hypothetical nigD-like protein K: Hypothetical nigD-like protein L: Hypothetical nigD-like protein hetero molecules
Mass: 18.015 Da / Num. of mol.: 1222 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT (RESIDUES 23-235) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 23-235) 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
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.87 Å3/Da / Density % sol: 57.12 %
Resolution: 2.42→29.712 Å / Num. all: 121998 / Num. obs: 121998 / % possible obs: 99.9 % / Redundancy: 4.3 % / Rsym value: 0.096 / Net I/σ(I): 9.8
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
2.42-2.48
4.2
0.779
1
38299
9058
0.779
100
2.48-2.55
4.2
0.636
1.2
37390
8824
0.636
100
2.55-2.62
4.2
0.51
1.5
36109
8533
0.51
100
2.62-2.71
4.2
0.403
1.9
35350
8336
0.403
100
2.71-2.79
4.2
0.329
2.3
34048
8022
0.329
100
2.79-2.89
4.2
0.268
2.8
33033
7773
0.268
100
2.89-3
4.3
0.204
3.7
32265
7583
0.204
100
3-3.12
4.3
0.177
4.3
30670
7199
0.177
100
3.12-3.26
4.3
0.131
5.7
29537
6916
0.131
100
3.26-3.42
4.3
0.099
7.3
28365
6656
0.099
100
3.42-3.61
4.3
0.088
7.9
27017
6327
0.088
100
3.61-3.83
4.3
0.077
8.8
25357
5936
0.077
100
3.83-4.09
4.3
0.065
10.2
24128
5631
0.065
100
4.09-4.42
4.3
0.056
11.5
22334
5210
0.056
100
4.42-4.84
4.3
0.05
12.9
20487
4780
0.05
100
4.84-5.41
4.3
0.054
11.6
18701
4358
0.054
100
5.41-6.25
4.3
0.063
10.6
16402
3821
0.063
100
6.25-7.65
4.3
0.068
9.3
13848
3223
0.068
100
7.65-10.82
4.3
0.052
10
10729
2506
0.052
100
10.82-29.712
4.2
0.043
10.7
5509
1306
0.043
95.4
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
MolProbity
3beta29
modelbuilding
PDB_EXTRACT
3.1
dataextraction
SOLVE
phasing
SCALA
3.3.15
datascaling
BUSTER-TNT
2.8.0
refinement
MOSFLM
datareduction
BUSTER
2.8.0
refinement
Refinement
Method to determine structure: MAD / Resolution: 2.42→29.712 Å / Cor.coef. Fo:Fc: 0.9393 / Cor.coef. Fo:Fc free: 0.9259 / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0 Details: 1. 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 ...Details: 1. 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. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 4. CHLORIDE (CL) AND ETHYLENE GLYCOL (EDO) MODELED ARE PRESENT PROTEIN BUFFER. 5. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS).
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