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1P43

REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsENRAF-NONIUS FR591
Temperature [K]110
Detector technologyCCD
Collection date2002-10-23
DetectorBRUKER PROTEUM
Wavelength(s)1.5418
Spacegroup nameP 21 21 2
Unit cell lengths107.300, 115.100, 72.400
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 1.800
R-factor0.185
Rwork0.185
R-free0.21300
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.005
RMSD bond angle1.200
Data reduction softwareLSCALE ((Bruker Nonius))
Data scaling softwareSAINT
Phasing softwareMOLREP
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000
High resolution limit [Å]1.8001.800
Rmerge0.047

*

0.217

*

Total number of observations303129

*

Number of reflections83994
Completeness [%]99.099
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Batch method

*

8293PEG 8000, potassium chloride, HEPPS, pH 8.0, Batch, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein10 (mg/ml)
211PEG800013 (%)
3110.25 (M)
411HEPPS/KCH25 (mM)pH8.0
511PEP3.5 (mM)
6113.5 (mM)

220113

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