2MSP

MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1997-01
Detector	MARRESEARCH
Spacegroup name	P 41 21 2
Unit cell lengths	79.660, 79.660, 463.790
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 3.300
R-factor	0.22
Rwork	0.218
R-free	0.26300 *
Structure solution method	MOLECULAR REPLACEMENT AND SINGLE ISOMORPHOUS REPLACEMENT
Starting model (for MR)	1msp
RMSD bond length	0.021
RMSD bond angle	21.900 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	TNT (5D)

Data quality characteristics

	Overall
Low resolution limit [Å]	50.000
High resolution limit [Å]	3.300
Rmerge	0.118
Total number of observations	279016 *
Number of reflections	23854
<I/σ(I)>	5.7
Completeness [%]	100.0
Redundancy	11.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.4 *	20 *	PROTEIN WAS CRYSTALLIZED FROM 16% PEG 6000, 80MM AMMONIUM SULFATE, 100MM TRIS - HCL, PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	drop	ammonium sulfate	40 (mM)
3	1	drop	Tris-HCl	5 (mM)
4	1	drop	dithiothreitol	1 (mM)
5	1	reservoir	PEG6000	16 (%)
6	1	reservoir	ammonium sulfate	80 (mM)
7	1	reservoir	Tris-HCl	100 (mM)