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1FB5

LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-02-10
DetectorMARRESEARCH
Spacegroup nameP 43 3 2
Unit cell lengths184.700, 184.700, 184.700
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 3.500
R-factor0.219
Rwork0.212
R-free0.25000

*

RMSD bond length0.010
RMSD bond angle23.400

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]500.0003.920
High resolution limit [Å]3.5003.510
Rmerge0.1600.320
Number of reflections13959
<I/σ(I)>4.3
Completeness [%]98.299.5
Redundancy104.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.4

*

2988% PEG 4000, 0.1 M Na acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298.K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein7-9 (mg/ml)
21reservoirTris-HCl10 (mM)pH7.4
31reservoirsodium acetate0.1 (M)
41reservoirPEG40008 (%(w/v))pH4.6

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