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1AH5

REDUCED FORM SELENOMETHIONINE-LABELLED HYDROXYMETHYLBILANE SYNTHASE DETERMINED BY MAD

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.5
Synchrotron siteSRS
BeamlinePX9.5
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1993-07
DetectorMARRESEARCH
Spacegroup nameP 21 21 2
Unit cell lengths88.470, 76.150, 50.790
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 2.400
R-factor0.168
Rwork0.168
R-free0.23500
Structure solution methodMAD
RMSD bond length0.009
RMSD bond angle23.462

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareMLPHARE
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]8.0002.460
High resolution limit [Å]2.4002.400
Rmerge0.0540.134
Number of reflections13486
<I/σ(I)>11.45.4
Completeness [%]99.098
Redundancy43.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP5.3PROTEIN WAS CRYSTALLISED AT PH 5.3 IN SITTING DROPS OF 0.05ML WITH 6-7MG/ML OF PROTEIN, 0.3MM EDTA, 15MM DITHIOTHREITOL, 10%(W/V) PEG6000 AND 0.01% NAN3 IN 0.1M NAAC., vapor diffusion - sitting drop
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6-7 (mg/ml)
21dropEDTA0.3 (mM)
31dropdithiothreitol15 (mM)
41dropPEG600010 (%(w/v))
51drop0.01 (%)
61dropsodium acetate0.1 (M)
71reservoirdithiothreitol10-20mg

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