1FXO

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2000-03-03
Detector	MARRESEARCH
Spacegroup name	P 1
Unit cell lengths	71.494, 73.064, 134.738
Unit cell angles	89.93, 80.92, 81.11

Refinement procedure

Resolution	73.000 - 1.660
R-factor	0.145
Rwork	0.142
R-free	0.19600
Structure solution method	Phase extension in DM
Starting model (for MR)	MAD structure (1G23)
RMSD bond length	0.016
RMSD bond angle	2.320 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SOLVE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.120	1.740
High resolution limit [Å]	1.660	1.660
Rmerge	0.053	0.332
Total number of observations	1141819 *
Number of reflections	297160 *
<I/σ(I)>	10.9	2
Completeness [%]	94.2	81.2
Redundancy	3.8	2

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)