SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ... SEQUENCE 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.
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Nov 19, 2007 / Details: Flat mirror (vertical focusing)
Radiation
Monochromator: Single crystal Si(111) bent (horizontal focusing) Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.97932
1
2
0.91837
1
Reflection
Resolution: 1.75→29.553 Å / Num. obs: 55436 / % possible obs: 99.7 % / Redundancy: 3.7 % / Biso Wilson estimate: 19.79 Å2 / Rmerge(I) obs: 0.102 / Rsym value: 0.102 / Net I/σ(I): 5.2
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
1.75-1.8
3.7
0.643
1.2
14990
4067
0.643
100
1.8-1.84
3.7
0.54
1.4
14585
3950
0.54
100
1.84-1.9
3.7
0.439
1.7
14304
3864
0.439
100
1.9-1.96
3.7
0.328
2.2
13806
3738
0.328
100
1.96-2.02
3.7
0.26
2.9
13380
3628
0.26
100
2.02-2.09
3.7
0.212
3.5
12948
3502
0.212
100
2.09-2.17
3.7
0.174
4.3
12673
3421
0.174
100
2.17-2.26
3.7
0.156
4.4
12019
3250
0.156
100
2.26-2.36
3.7
0.137
5.3
11765
3173
0.137
100
2.36-2.47
3.7
0.122
5.9
11174
3015
0.122
100
2.47-2.61
3.7
0.11
6.5
10633
2855
0.11
99.9
2.61-2.77
3.7
0.098
6.9
10146
2744
0.098
99.9
2.77-2.96
3.7
0.093
6.9
9375
2538
0.093
99.9
2.96-3.2
3.7
0.087
7.2
8864
2395
0.087
99.7
3.2-3.5
3.7
0.073
8.3
8185
2213
0.073
99.5
3.5-3.91
3.7
0.063
9.7
7377
1991
0.063
99.5
3.91-4.52
3.7
0.063
9.2
6477
1761
0.063
98.7
4.52-5.53
3.7
0.061
9.5
5494
1499
0.061
98.2
5.53-7.83
3.6
0.064
9.7
4174
1174
0.064
97.9
7.83-29.553
3.4
0.06
9.7
2221
658
0.06
94.1
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
SCALA
datascaling
PDB_EXTRACT
3
dataextraction
MAR345
CCD
datacollection
MOSFLM
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 1.75→29.553 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.946 / SU B: 4.072 / SU ML: 0.072 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.104 / ESU R Free: 0.103 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 RECORD CONTAINS RESIDUAL B FACTORS ONLY. 4. CDP AND MAGNESIUM ARE MODELED BASED ON ELECTRON DENSITY, HOMOLOGOUS STRUCTURES, COORDINATION AS WELL AS HYDROGEN BONDING. THE CDP DENSITY CAN ALSO FIT UDP, BUT WITH SLIGHTLY LESS FAVORABLE HYDROGEN BOND INTERACTIONS. 5. CHLORIDE, SODIUM, ETHYLENE GLYCOL (EDO) AND THIOCYNATE (SCN) ARE PRESENT IN THE CRYSTALLIZATION/CRYO CONDITIONS. 6. THE DENSITY FOR RESIDUES A32-33, B102-103 ARE POOR. THE MODEL WAS BUILT BASED ON THE OTHER WELL ORDERED SUBUNIT.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.201
2813
5.1 %
RANDOM
Rwork
0.166
-
-
-
obs
0.168
55402
99.54 %
-
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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