1914

SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID2
Synchrotron site	ESRF
Beamline	ID2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-09
Detector	MARRESEARCH
Wavelength(s)	0.900, 1.100
Spacegroup name	P 43 2 2
Unit cell lengths	69.020, 69.020, 90.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.530
R-factor	0.248
Rwork	0.248
R-free	0.29900
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
Data reduction software	DENZO
Data scaling software	CCP4
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.600
High resolution limit [Å]	2.530	2.530
Rmerge	0.069	0.022
Total number of observations	36956 *
Number of reflections	7634 *
<I/σ(I)>	5.8	2.4
Completeness [%]	98.7	97.2
Redundancy	5	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.7	4 *	THE SRPPHI14-9 PROTEIN WAS CRYSTALLIZED (BIRSE ET AL., FEBS LETTERS, 1996) BY THE HANGING DROP METHOD IN 2.0 M NAH2/K2H PO4, PH 7.7, 2% MPD, 1.0 MM NAN3 AT 4 DEGREES C WITH A FINAL PROTEIN CONCENTRATION OF 5-8 MG ML-1. CRYSTALS FORMED OVER 2-3 WEEKS AND WERE TYPICALLY 150 X 150 X 300 MM3 IN SPACE, hanging drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		2.0 (M)
2	1	reservoir	MPD	2 (%)
3	1	reservoir		1.0 (mM)
4	1	drop	protein	5-8 (mg/ml)