1X9J

Structure of butyrate kinase 2 reveals both open- and citrate-induced closed conformations: implications for substrate-induced fit conformational changes

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-ID-B
Synchrotron site	APS
Beamline	14-ID-B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-04-27
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.9793
Spacegroup name	P 43
Unit cell lengths	193.680, 193.680, 122.932
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	91.480 - 3.000
Rwork	0.261
R-free	0.28400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1saz
RMSD bond length	0.005
RMSD bond angle	1.000
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	3.110
High resolution limit [Å]	3.000	3.000
Number of reflections	88350
<I/σ(I)>	11.9	4.2
Completeness [%]	97.0	80.3
Redundancy	14.2	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	310	CRYSTALLIZATION CONDITIONS: THE PROTEIN SOLUTION CONTAINS 22.5-25 mg/ml BUK2, 25 mM TRIS-HCl pH 8.5, 400 mM NACl, 5 mM DTT, 10%(w/v) GLYCEROL. THE RESERVOIR SOLUTION IS 1ml of 77 mM PHOSPHATE-CITRATE AND 55% (w/v) PEG 200, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 310K