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1KV5

Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191 mutated to Ser

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX13
Temperature [K]100
Detector technologyCCD
Collection date2001-05-27
DetectorMARRESEARCH
Wavelength(s)0.8500
Spacegroup nameP 21 21 21
Unit cell lengths44.943, 100.638, 109.350
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 1.650
R-factor0.143

*

Rwork0.143
R-free0.17500

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)5tim
RMSD bond length0.013
RMSD bond angle1.770

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0001.680
High resolution limit [Å]1.6501.650
Rmerge0.0310.253
Total number of observations245458

*

Number of reflections60451

*

<I/σ(I)>37.75.4
Completeness [%]99.999.3
Redundancy4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5.5295ammonium sulfate, sodium chloride, citric acid, pH 5.5, VAPOR DIFFUSION, HANGING DROP at 295K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirammonium sulfate2 (M)
21reservoircitric acid0.1 (M)pH5.5
31reservoir0.2 (M)
41dropprotein3 (mg/ml)
51dropPGA10 (mM)

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PDB entries from 2024-03-27

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