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THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2000-02-29
Detector	MARRESEARCH
Spacegroup name	P 1
Unit cell lengths	71.656, 73.656, 134.469
Unit cell angles	89.98, 80.91, 80.91

Refinement procedure

Resolution	73.000 - 1.900
R-factor	0.18
Rwork	0.176
R-free	0.25100
RMSD bond length	0.025
RMSD bond angle	1.869
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	72.500	1.990
High resolution limit [Å]	1.900	1.900
Rmerge	0.054	0.286
Total number of observations	377690 *
Number of reflections	202988
<I/σ(I)>	9.2
Completeness [%]	96.1	95.6
Redundancy	1.9	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	293 *	Blankenfeldt, W., (2000) Acta Crystallogr.,Sect.D, 56, 1501. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	9-12 (%(w/v))
2	1	reservoir	lithium sulfate	0.5 (M)
3	1	reservoir	citrate/NaOH	0.1 (M)