1BU6

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	1994-08-15
Detector	SDMS
Spacegroup name	P 1 21 1
Unit cell lengths	91.900, 119.000, 109.300
Unit cell angles	90.00, 103.40, 90.00

Refinement procedure

Resolution	20.000 - 2.370
R-factor	0.167 *
Rwork	0.167
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1glf
RMSD bond length	0.019
RMSD bond angle	2.928
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]	37.000 *
High resolution limit [Å]	2.370
Rmerge	0.068
Total number of observations	132331 *
Number of reflections	69682
Completeness [%]	74.0
Redundancy	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5		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)