1CKA

STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK

Experimental procedure

Detector technology	IMAGE PLATE
Collection date	1994-07-16
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 41
Unit cell lengths	47.200, 47.200, 29.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 1.500
R-factor	0.174
Rwork	0.174
RMSD bond length	0.012
RMSD bond angle	1.900 *
Data reduction software	DENZO
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	1.500 *	1.500 *
Rmerge	0.040 *
Total number of observations	66868 *
Number of reflections	10512
Completeness [%]	81.3	73.8 *
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.6 *	21 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	85 (mg/ml)
2	1	drop	C3G	10 (mg/ml)
3	1	reservoir	sodium acetate	0.1 (M)
4	1	reservoir	ammonium acetate	0.2 (M)
5	1	reservoir	PEG4000	28-32 (%)