1BTK

PH DOMAIN AND BTK MOTIF FROM BRUTON'S TYROSINE KINASE MUTANT R28C

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-09-24
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	49.150, 59.870, 55.940
Unit cell angles	90.00, 98.21, 90.00

Refinement procedure

Resolution	40.500 - 1.600
R-factor	0.231
Rwork	0.231
R-free	0.28200
Structure solution method	SIRAS
RMSD bond length	0.110
RMSD bond angle	1.990
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.500	1.630
High resolution limit [Å]	1.600	1.600
Rmerge	0.054 *	0.236 *
Number of reflections	42840
<I/σ(I)>	11.7
Completeness [%]	99.9	99.3
Redundancy	4.4	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5		PROTEIN WAS CRYSTALLIZED FROM 32.5% PEG-3350, 200 MM MGCL2, 500 MM NACL, 100 MM TRIS-HCL, PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3350	32.5 (%(w/v))
2	1	reservoir	Tris-HCl	100 (mM)
3	1	reservoir		200 (mM)
4	1	reservoir		500 (mM)