1F6D

THE STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE FROM E. COLI.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	1999-02-20
Detector	BRANDEIS
Spacegroup name	P 1 21 1
Unit cell lengths	91.008, 94.541, 100.970
Unit cell angles	90.00, 109.13, 90.00

Refinement procedure

Resolution	30.320 - 2.500
R-factor	0.198
Rwork	0.198
R-free	0.27100
RMSD bond length	0.009
RMSD bond angle	23.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.051	0.210
Total number of observations	163518 *
Number of reflections	50775	2386 *
<I/σ(I)>	21.6
Completeness [%]	93.1	89
Redundancy	3.2	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.3	298	13 % PEG 8000, 0.3 M NaCl, 0.1 M sodium citrate, pH 5.3, VAPOR DIFFUSION, temperature 298K
1	Vapor diffusion, hanging drop *	5.3	298	13 % PEG 8000, 0.3 M NaCl, 0.1 M sodium citrate, pH 5.3, VAPOR DIFFUSION, temperature 298K
1	Vapor diffusion, hanging drop *	5.3	298	13 % PEG 8000, 0.3 M NaCl, 0.1 M sodium citrate, pH 5.3, VAPOR DIFFUSION, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	4 (mg/ml)
2	1	reservoir	PEG8000	13 (%)
3	1	reservoir	sodium chloride	0.3 (M)
4	1	reservoir	sodium citrate	0.1 (M)
5	1	reservoir	UDP-GlcNAc	0.1 (M)