1G2V

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-07-31
Detector	RIGAKU RAXIS
Spacegroup name	P 1 21 1
Unit cell lengths	73.017, 134.361, 140.901
Unit cell angles	90.00, 98.22, 90.00

Refinement procedure

Resolution	100.000 - 2.600
R-factor	0.217
Rwork	0.215
R-free	0.24200
Starting model (for MR)	1g1l
RMSD bond length	0.028
RMSD bond angle	2.270 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.740
High resolution limit [Å]	2.600	2.600
Rmerge	0.070	0.154
Total number of observations	310827 *
Number of reflections	75557 *
<I/σ(I)>	7.4	4.6
Completeness [%]	91.5	60.1
Redundancy	4.1	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	292	5% (w/v) PEG 6000, 0.1 M Na-citrate pH 4.0; protein incubated with 10 mM dTTP, pH 4.00, VAPOR DIFFUSION, SITTING DROP, temperature 292K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	5 (%(w/v))
2	1	reservoir	Na citrate	0.1 (M)
3	1	reservoir	PEG600	25 (%(v/v))