1HM8

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-04-11
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9326
Spacegroup name	H 3
Unit cell lengths	92.459, 92.459, 279.562
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	39.630 - 2.500
R-factor	0.184
Rwork	0.184
R-free	0.24300
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.011
RMSD bond angle	25.100 *
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.560
High resolution limit [Å]	2.500	2.500
Rmerge	0.024 *	0.069
Total number of observations	73418 *
Number of reflections	29218
<I/σ(I)>	23.1	10.8
Completeness [%]	94.7	96.6
Redundancy	2.5	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	20 *	18 % PEG 400 (w/w) 300 mM CaCl2 50 mM NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	13 (mg/ml)
2	1	reservoir	PEG400	26 (%(v/v))
3	1	reservoir		50 (mM)
4	1	reservoir		300 (mM)	pH8.0