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1K8X

Crystal Structure Of AlphaT183V Mutant Of Tryptophan Synthase From Salmonella Typhimurium

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]100
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Wavelength(s)0.8345
Spacegroup nameC 1 2 1
Unit cell lengths182.220, 59.990, 67.070
Unit cell angles90.00, 94.68, 90.00
Refinement procedure
Resolution19.600

*

- 1.900
Rwork0.192
R-free0.23200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qop
RMSD bond length0.008
RMSD bond angle1.400
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.9002.000
High resolution limit [Å]1.9001.900
Rmerge0.076

*

0.261

*

Total number of observations112612

*

Number of reflections50864

*

Completeness [%]90.192.1

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.8296PEG 8000, EDTA, spermine, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 296K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
101reservoirspermine2 (mM)
111reservoirPEG80008-12 (%(w/v))
21dropNa+-bicine50 (mM)pH7.8
31dropNa+-EDTA10 (mM)
41dropdithioerythritol1 (mM)
51dropPLP20000 (nM)
61reservoirNa+-bicine50 (mM)pH7.8
71reservoirdithioerythritol5 (mM)
81reservoirNa+-EDTA5 (mM)
91reservoirPLP0.1 (mM)

229380

PDB entries from 2024-12-25

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