1GLF

CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1990-08-01
Detector	SDMS
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	92.100, 117.400, 108.400
Unit cell angles	90.00, 93.10, 90.00

Refinement procedure

Resolution	20.000 - 2.620
R-factor	0.146 *
Rwork	0.146
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gla
RMSD bond length	0.020
RMSD bond angle	20.904 *
Data reduction software	SDMS
Data scaling software	SDMS
Phasing software	FRFSUM ((WOLFGANG KABSCH))
Refinement software	TNT (5F-6)

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.620
Rmerge	0.076
Total number of observations	190143 *
Number of reflections	58942
Completeness [%]	84.0
Redundancy	3.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5		Faber, H.R., (1989) J. Mol. Biol., 207, 637. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-30 (mg/ml)
2	1	drop	sodium potassium phosphate	50 (mM)
3	1	drop	glycerol	10 (mM)
4	1	drop	beta-mercaptoethanol	2 (mM)
5	1	reservoir		300-500 (mM)
6	1	reservoir	PEG1550	20 (%(w/w))	PEG1550 to 20000
7	1	reservoir	sodium potassium phosphate	50 (mM)
8	1	drop	ADP	100 (mM)