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1LOO

Crystal Structure of the Mouse-Muscle Adenylosuccinate Synthetase Ligated with GTP

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2002-03-19
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameP 43 21 2
Unit cell lengths69.935, 69.935, 198.090
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 2.200
Rwork0.244
R-free0.27600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1j4b
RMSD bond length0.006
RMSD bond angle1.200

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Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]65.9002.280
High resolution limit [Å]2.2002.200
Rmerge0.081

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0.312

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Total number of observations126081

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Number of reflections25715

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<I/σ(I)>202.3
Completeness [%]89.5

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98.5

*

Redundancy4.94
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5

*

296PEG 8000, magnesium acetate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 296K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropenzyme10 (mg/ml)
21dropHEPES50 (mM)pH7.5
31drop50 (mM)
41dropdithiothreitol1 (mM)
51dropEDTA0.5 (mM)
61dropGTP5 (mM)
71reservoirmagnesium acetate200 (mM)
81reservoirHEPES100 (mM)pH7.0
91reservoirPEG800018 (%(w/v))

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PDB entries from 2024-05-15

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