1NOH

The structure of bacteriophage phi29 scaffolding protein gp7 after prohead assembly

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2001-11-17
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	C 2 2 21
Unit cell lengths	114.005, 117.301, 105.933
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.150 - 2.800
R-factor	0.254
Rwork	0.254
R-free	0.29000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1no4
RMSD bond length	0.007 *
RMSD bond angle	1.160 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.150	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.091 *	0.473 *
Number of reflections	17904 *
<I/σ(I)>	11.5	2.4
Completeness [%]	98.2	95.9
Redundancy	14.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6.5	298	14.4 % Peg 8000, 0.08 M sodium cacodylate, 0.16 M calcium acetate, 20 % glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	PEG8000	14.4 (%(v/v))
2	1	1	sodium cacodylate	0.08 (M)	pH6.5
3	1	1	cadmium acetate	0.16 (M)
4	1	1	glycerol	20 (%(v/v))
5	1	1	protein	1 (mg/ml)