1O6Y

Catalytic domain of PknB kinase from Mycobacterium tuberculosis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2002-05-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	114.607, 122.088, 46.975
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	61.000 - 2.200
R-factor	0.1927
Rwork	0.191
R-free	0.23030
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1phk
RMSD bond length	0.017
RMSD bond angle	1.623
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	61.000 *	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.090 *	0.640 *
Number of reflections	17152
<I/σ(I)>	6.7	1.3
Completeness [%]	99.8	99.8
Redundancy	8	8.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	19 *	PROTEIN CRYSTALLIZED FROM 27% PEG 400, 4% 1,3-BUTANEDIOL, 100 MM HEPES, PH 7.5, 30 MM MGCL2 AT 19 DEGREES C

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	HEPES	0.1 (M)	pH7.5
3	1	reservoir		30 (mM)
4	1	reservoir	AMP-PCP	150000 (mM)
5	1	reservoir	PEG400	27 (%)
6	1	reservoir	1,3-butanediol	4 (%)