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3GAR

A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE

Experimental procedure
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]90
Detector technologyIMAGE PLATE
Collection date1997-03
DetectorMARRESEARCH
Spacegroup nameP 61 2 2
Unit cell lengths50.400, 50.400, 275.500
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution50.000 - 1.900
R-factor0.215
Rwork0.215
R-free0.27400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gar
RMSD bond length0.006
RMSD bond angle26.900

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.8)
Refinement softwareX-PLOR (3.8)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.970
High resolution limit [Å]1.8001.900
Rmerge0.0500.331
Total number of observations67156

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Number of reflections16340
<I/σ(I)>22.62.6
Completeness [%]92.881.8
Redundancy4.12.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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7.522

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CRYSTAL GREW FROM A SOLUTION OF 2%(V/V) PEG 400. 2.0M AMMONIUM SULFATE, 0.1M HEPES, PH 7.5
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21reservoirPEG4002 (%(v/v))
31reservoirammonium sulfate2.0 (M)
41reservoirsodium HEPES0.1 (M)

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PDB entries from 2024-05-15

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