1HM9

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	2000-05-16
Detector	MARRESEARCH
Spacegroup name	H 3
Unit cell lengths	89.509, 89.509, 278.753
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.140 - 1.750
R-factor	0.183
Rwork	0.183
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hm8
RMSD bond length	0.011
RMSD bond angle	24.600 *
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.800
High resolution limit [Å]	1.750	1.750
Rmerge	0.046	0.354
Total number of observations	187478 *
Number of reflections	82248	5926
<I/σ(I)>	12.3	1.9
Completeness [%]	97.9	96.4
Redundancy	2.3	2

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