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1HM8

CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
Collection date2000-04-11
DetectorADSC QUANTUM 4
Wavelength(s)0.9326
Spacegroup nameH 3
Unit cell lengths92.459, 92.459, 279.562
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution39.630 - 2.500
R-factor0.184
Rwork0.184
R-free0.24300
Structure solution methodFOURIER SYNTHESIS
RMSD bond length0.011
RMSD bond angle25.100

*

Data reduction softwareDENZO
Data scaling softwareCCP4 ((SCALA))
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.0002.560
High resolution limit [Å]2.5002.500
Rmerge0.024

*

0.069
Total number of observations73418

*

Number of reflections29218
<I/σ(I)>23.110.8
Completeness [%]94.796.6
Redundancy2.51.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP820

*

18 % PEG 400 (w/w) 300 mM CaCl2 50 mM NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein13 (mg/ml)
21reservoirPEG40026 (%(v/v))
31reservoir50 (mM)
41reservoir300 (mM)pH8.0

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PDB entries from 2024-05-29

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