Mass: 18.015 Da / Num. of mol.: 312 / 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: 2.94 Å3/Da / Density % sol: 58.18 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 1.6000M (NH4)2SO4, 0.1000M NaCl, 0.1M HEPES pH 7.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jun 11, 2009 / Details: Flat mirror (vertical focusing)
Radiation
Monochromator: Single crystal Si(111) bent monochromator (horizontal focusing) Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97864 Å / Relative weight: 1
Reflection
Resolution: 1.95→29.412 Å / Num. obs: 33717 / % possible obs: 100 % / Redundancy: 5.5 % / Biso Wilson estimate: 27.798 Å2 / Rmerge(I) obs: 0.086 / Rsym value: 0.086 / Net I/σ(I): 14
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
1.95-2
5.6
0.577
1.3
13703
2466
0.577
100
2-2.06
5.6
0.453
1.7
13262
2380
0.453
100
2.06-2.12
5.6
0.355
2.1
13035
2344
0.355
100
2.12-2.18
5.6
0.287
2.7
12492
2246
0.287
100
2.18-2.25
5.6
0.233
3.3
12237
2196
0.233
100
2.25-2.33
5.6
0.198
3.8
12009
2151
0.198
100
2.33-2.42
5.6
0.168
4.5
11430
2049
0.168
100
2.42-2.52
5.6
0.151
4.9
11070
1992
0.151
100
2.52-2.63
5.6
0.135
5.5
10591
1903
0.135
100
2.63-2.76
5.6
0.108
6.6
10134
1821
0.108
100
2.76-2.91
5.6
0.095
7.3
9719
1744
0.095
100
2.91-3.08
5.5
0.079
8.5
9058
1637
0.079
100
3.08-3.3
5.5
0.074
8.6
8640
1563
0.074
100
3.3-3.56
5.5
0.068
9.4
8015
1469
0.068
100
3.56-3.9
5.4
0.063
9.2
7250
1337
0.063
100
3.9-4.36
5.4
0.055
11.1
6611
1218
0.055
100
4.36-5.03
5.3
0.055
10.7
5854
1096
0.055
100
5.03-6.17
5.3
0.061
10.1
4886
930
0.061
100
6.17-8.72
5
0.059
9.2
3734
742
0.059
100
8.72-29.41
4.6
0.047
11.2
1999
433
0.047
97.5
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Phasing
Phasing
Method: SAD
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Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SOLVE
phasing
MolProbity
3beta29
modelbuilding
SCALA
3.2.5
datascaling
PDB_EXTRACT
3.006
dataextraction
MOSFLM
datareduction
Refinement
Method to determine structure: SAD / Resolution: 1.95→29.412 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.951 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 5.154 / SU ML: 0.078 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.126 / ESU R Free: 0.115 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. CL IONS AND GLYCEROL MOLECULES ARE MODELED BASED ON CRYSTALLIZATION AND CRYOPROTECTION CONDITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.188
1706
5.1 %
RANDOM
Rwork
0.163
-
-
-
obs
0.164
33677
99.96 %
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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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