SIGNALING PROTEIN / FecR protein / PF04773 family / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
Mass: 18.015 Da / Num. of mol.: 91 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT (RESIDUES 107-337) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG ...THE CONSTRUCT (RESIDUES 107-337) WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. THE THR AT POSITION 199 OF THE CONSTRUCT WAS MUTATED TO GLY.
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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: 2.64 Å3/Da / Density % sol: 53.4 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 4.300M sodium chloride, 0.1M HEPES pH 7.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 8, 2011 Details: Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing)
Radiation
Monochromator: single crystal Si(111) bent / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.91837
1
2
0.97963
1
3
0.9791
1
Reflection
Resolution: 2.5→29.449 Å / Num. all: 20436 / Num. obs: 20436 / % possible obs: 99.7 % / Redundancy: 5.7 % / Rsym value: 0.11 / Net I/σ(I): 11.2
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
2.5-2.56
6.1
0.834
2.1
9037
1476
0.834
100
2.56-2.64
5.9
0.658
2.6
8490
1450
0.658
99.9
2.64-2.71
5.7
0.546
3
7959
1395
0.546
99.8
2.71-2.8
5.6
0.477
3.4
7652
1364
0.477
99.3
2.8-2.89
4.8
0.358
4.1
6366
1320
0.358
99.9
2.89-2.99
5.8
0.297
5.2
7532
1308
0.297
100
2.99-3.1
6.1
0.235
6.9
7590
1239
0.235
100
3.1-3.23
6.1
0.177
8.8
7264
1189
0.177
99.9
3.23-3.37
6
0.137
11.1
6975
1161
0.137
99.9
3.37-3.54
5.9
0.104
13.8
6429
1095
0.104
100
3.54-3.73
5.2
0.088
14.3
5496
1055
0.088
99
3.73-3.95
5.5
0.072
17.1
5500
999
0.072
99.8
3.95-4.23
6.2
0.063
21.7
5967
960
0.063
99.9
4.23-4.56
6
0.052
25.2
5225
864
0.052
99.8
4.56-5
5.9
0.051
25.2
4840
825
0.051
99.9
5-5.59
4.7
0.057
19.3
3559
750
0.057
99.2
5.59-6.46
5.7
0.071
20.4
3819
670
0.071
99.6
6.46-7.91
5.8
0.078
19.9
3365
578
0.078
99.5
7.91-11.18
4.7
0.042
24.8
2185
465
0.042
99.6
11.18-29.449
5.4
0.049
27.1
1469
273
0.049
94.4
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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
SHELX
phasing
SHARP
phasing
SCALA
3.3.20
datascaling
BUSTER-TNT
2.10.0
refinement
MOSFLM
datareduction
SHELXD
phasing
BUSTER
2.10.0
refinement
Refinement
Method to determine structure: MAD / Resolution: 2.5→29.449 Å / Cor.coef. Fo:Fc: 0.9389 / Cor.coef. Fo:Fc free: 0.9243 / Occupancy max: 1 / Occupancy min: 0.37 / 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. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 4. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS). 5.CHLORIDE IONS (CL) FROM THE CRYSTALLIZATION AND GLYCEROL USED AS A CRYOPROTECTANT WERE MODELED INTO THE STRUCTURE.
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