1A37

14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-06
Detector	RIGAKU RAXIS IV
Spacegroup name	P 65
Unit cell lengths	94.730, 94.730, 250.870
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 3.600
R-factor	0.31 *
Rwork	0.320
R-free	0.36000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.020 *
RMSD bond angle	2.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.800
High resolution limit [Å]	3.600	3.600
Rmerge	0.070 *
Number of reflections	14696 *
<I/σ(I)>	20	7
Completeness [%]	99.5 *	98.8
Redundancy	4.3	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	4 *	Liu, D., (1995) Nature, 376, 191. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5-10 (mg/ml)
2	1	reservoir	PEG3500	20-24 (%)
3	1	reservoir	Tris-HCl	100 (mM)
4	1	reservoir		10 (mM)
5	1	reservoir		1 (mM)