CRYSTAL PACKING ANALYSIS AND SIZE EXCLUSION CHROMATOGRAPHY COMBINED WITH STATIC LIGHT SCATTERING SUGGEST THE ASSIGNMENT OF A TETRAMER AS THE SIGNIFICANT OLIGOMERIC FORM IN SOLUTION UNDER THE CONDITIONS TESTED.
-
Components
#1: Protein
putativecarboxypeptidase /
Mass: 46063.512 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Burkholderia mallei ATCC 23344 (bacteria) Gene: BMA1798 / Plasmid: SpeedET / Production host: Escherichia coli (E. coli) / Strain (production host): HK100 / References: UniProt: Q62IR3, UniProt: A0A0H2WJQ2*PLUS
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: May 7, 2009 Details: Flat mirror, vertical and horizontal focussing mirrors
Radiation
Monochromator: Double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97931 Å / Relative weight: 1
Reflection
Resolution: 2.49→29.553 Å / Num. obs: 34624 / % possible obs: 99.1 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 61.88 Å2 / Rmerge(I) obs: 0.076 / Net I/σ(I): 15.45
Reflection shell
Resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
Diffraction-ID
% possible all
2.49-2.58
0.78
2.1
30530
6209
1
92
2.58-2.68
0.575
2.9
32970
6413
1
99.9
2.68-2.8
0.431
3.8
33733
6537
1
99.8
2.8-2.95
0.285
5.8
34715
6735
1
100
2.95-3.14
0.18
8.9
35230
6829
1
99.9
3.14-3.38
0.109
13.9
33889
6568
1
100
3.38-3.71
0.069
20.9
33208
6469
1
100
3.71-4.25
0.05
26.9
34295
6715
1
100
4.25-5.33
0.04
32.4
33346
6575
1
100
5.33-29.553
0.035
35.6
34147
6757
1
99.4
-
Phasing
Phasing
Method: SAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.5.0053
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
XSCALE
datascaling
PDB_EXTRACT
3.006
dataextraction
XDS
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: SAD / Resolution: 2.49→29.553 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.958 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 9.767 / SU ML: 0.096 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.16 / ESU R Free: 0.148 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.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. 4.CHLORIDE (CL) AND GLYCEROL (GOL) FROM THE CRYSTALLIZATION AND CRYOPROTECTION SOLUTION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE. 5.THE RAMACHANDRAN OUTLIER AT GLN39 IS SUPPORTED BY ELECTRON DENSITY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.185
1742
5 %
RANDOM
Rwork
0.156
-
-
-
obs
0.157
34608
99.51 %
-
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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