1G3L

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-03-01
Detector	RIGAKU RAXIS
Spacegroup name	P 21 21 21
Unit cell lengths	71.087, 138.557, 139.676
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	100.000 - 2.700
R-factor	0.205
Rwork	0.204
R-free	0.23000
Starting model (for MR)	1g1l
RMSD bond length	0.014
RMSD bond angle	2.390 *
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]	49.900	2.840
High resolution limit [Å]	2.700	2.800
Rmerge	0.120	0.266
Total number of observations	260832 *
Number of reflections	36311
<I/σ(I)>	6.8	2.9
Completeness [%]	94.2	70.8
Redundancy	7.2	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	292	10 % (w/v) PEG 6000, 0.2 M Li-sulfate, 0.1 M Na-citrate pH 4.0; protein incubated with 10 mM dTDP-L-rhamnose, VAPOR DIFFUSION, SITTING DROP, temperature 292K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	10 (%(w/v))
2	1	reservoir		0.2 (M)
3	1	reservoir	Na citrate	0.1 (M)