A: LINE-1 type transposase domain-containing protein 1 B: LINE-1 type transposase domain-containing protein 1 C: LINE-1 type transposase domain-containing protein 1 hetero molecules
Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
Sequence details
1. THE CONSTRUCT (RESIDUES 235-321) WAS EXPRESSED WITH A N-TERMINAL PURIFICATION TAG ...1. THE CONSTRUCT (RESIDUES 235-321) WAS EXPRESSED WITH A N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. 2. THE PROTEIN WAS REDUCTIVELY METHYLATED PRIOR TO CRYSTALLIZATION.
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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: 3.27 Å3/Da / Density % sol: 62.39 % Description: While data were scaled with XSCALE, the final statistics reported in the REMARK 200 section have been calculated with SCALA with fixed scales and no sd correction.
Resolution: 2.73→48.712 Å / Num. all: 11913 / Num. obs: 11913 / % possible obs: 99.8 % / Redundancy: 6.7 % / Rsym value: 0.063 / Net I/σ(I): 15.2
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
2.73-2.88
7
0.598
1.3
11721
1679
0.598
99.9
2.88-3.05
7
0.35
2.2
10944
1570
0.35
99.9
3.05-3.26
6.9
0.203
3.8
10501
1511
0.203
100
3.26-3.52
6.8
0.115
6.2
9636
1415
0.115
99.9
3.52-3.86
6.8
0.083
8.2
8928
1310
0.083
100
3.86-4.32
6.6
0.053
10
7987
1204
0.053
99.9
4.32-4.98
6.5
0.039
14.2
6991
1073
0.039
100
4.98-6.1
6.3
0.039
15.3
5854
927
0.039
100
6.1-8.63
5.9
0.036
16.2
4510
766
0.036
100
8.63-48.712
4.8
0.028
22.5
2182
458
0.028
96.7
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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
XSCALE
datascaling
BUSTER-TNT
2.8.0
refinement
XDS
datareduction
SHELXD
phasing
BUSTER
2.8.0
refinement
Refinement
Method to determine structure: MAD / Resolution: 2.73→48.712 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.9186 / 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. SULFATE, CHLORIDE MODELED ARE PRESENT IN PROTEIN/CRYSTALLIZATION/ CRYO CONDITIONS. 4. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS). 5. THE PROTEIN WAS SUBJECTED TO REDUCTIVE METHYLATION PRIOR TO CRYSTALLIZATION AND LYSINES HAVE BEEN MODELED AS N-DIMETHYL-LYSINE (MLY). HOWEVER, METHYL GROUPS ON LYSINES WERE NOT MODELED DUE TO POOR SIDE-CHAIN DENSITY.
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