1E8C

Structure of MurE the UDP-N-acetylmuramyl tripeptide synthetase from E. coli

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	110
Detector technology	CCD
Collection date	1999-11-15
Detector	MARRESEARCH
Wavelength(s)	0.9791,0.9790,0.8550,0.93
Spacegroup name	C 2 2 21
Unit cell lengths	93.465, 99.690, 236.146
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.730 - 2.000
R-factor	0.202
Rwork	0.202
R-free	0.23000
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	23.500 *
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]	46.700	2.130
High resolution limit [Å]	2.000	2.000
Rmerge	0.066 *	0.220 *
Total number of observations	323548 *
Number of reflections	72674 *
Completeness [%]	98.3	91.2
Redundancy	4.5	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5		HANGING DROP EXPERIMENT RESERVOIR: 13% PEG MME 5K, 0.5M LICL, 10% ISOPROPANOL, 0.1M HEPES PH 7.5, 5MM DTT, 1MM UDP-TRIPEPTIDE DROP: 2UL PROTEIN SOLUTION (MURE @ 10MGML-1 IN 20MM HEPES PH 7.5, 200MM NACL, 5MM DTT) WITH 2UL RESERVOIR SOLUTION.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
10	1	reservoir	dithiothreitol	5 (mM)
2	1	drop	HEPES	20 (mM)
3	1	drop		200 (mM)
4	1	drop	dithiothreitol	5 (mM)
5	1	drop	UMT	1 (mM)
6	1	reservoir	HEPES	0.1 (M)
7	1	reservoir	PEG MME5000	13 (%)
8	1	reservoir		0.5 (M)
9	1	reservoir	iso-propanol	10 (%)