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1I9C

GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]103
Detector technologyIMAGE PLATE
Collection date1999-08-15
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths64.348, 113.139, 108.439
Unit cell angles90.00, 96.00, 90.00
Refinement procedure
Resolution30.000 - 1.900
R-factor0.168

*

Rwork0.168
R-free0.22100
Structure solution methodRIGID BODY REFINEMENT
Starting model (for MR)1ccw
RMSD bond length0.008
RMSD bond angle0.025
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.940
High resolution limit [Å]1.9001.900
Rmerge0.0730.281
Total number of observations555148

*

Number of reflections1216808102

*

<I/σ(I)>18.45
Completeness [%]99.9100
Redundancy4.63.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP4.5

*

293PEG-4000, cadmium chloride, coenzyme B12, sodium glutamate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein3.5 (mg/ml)
21dropcoenzyme B120.5 (mg/ml)
31drop2 (mM)
41reservoirPEG40006 (%(w/v))
51reservoirNa-S-glutamate0.1 (M)pH4.5

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PDB entries from 2024-05-15

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