1G3P

CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-09
Detector	MAR scanner 345 mm plate
Spacegroup name	P 32 2 1
Unit cell lengths	48.681, 48.681, 153.222
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 1.460
R-factor	0.187
Rwork	0.187
R-free	0.22500
Structure solution method	SIRAS (USING MAD X-RAY DATA)
RMSD bond length	0.009
RMSD bond angle	27.019 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELX-97
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	22.000	1.510
High resolution limit [Å]	1.460	1.460
Rmerge	0.034 *	0.110 *
Total number of observations	282603 *
Number of reflections	37511
<I/σ(I)>	27	8.5
Completeness [%]	99.8	99.2
Redundancy	7.53	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6.5		EQUAL VOLUMES OF THE PROTEIN SOLUTION (10 MG/ML) BUFFERED WITH 50 MM PIPES PH 6.5 AND THE PRECIPITANT (30% PEG 4000, 0.2 M AMMONIUM SULFATE, 2 MM DTT) WERE MIXED AND EQUILIBRATED (IN THE HANGING DROP SETUP) AGAINST THE PRECIPITANT., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	N1-N2	10 (mg/ml)
2	1	2	ammonium sulfate	0.2 (M)
3	1	2	PEG4000	30 (%(w/v))
4	1	2	DTT	2 (mM)
5	1	2	PIPES	50 (mM)