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2MSP

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

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.5
Synchrotron siteSRS
BeamlinePX9.5
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1997-01
DetectorMARRESEARCH
Spacegroup nameP 41 21 2
Unit cell lengths79.660, 79.660, 463.790
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 3.300
R-factor0.22
Rwork0.218
R-free0.26300

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Structure solution methodMOLECULAR REPLACEMENT AND SINGLE ISOMORPHOUS REPLACEMENT
Starting model (for MR)1msp
RMSD bond length0.021
RMSD bond angle21.900

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Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareAMoRE
Refinement softwareTNT (5D)
Data quality characteristics
 Overall
Low resolution limit [Å]50.000
High resolution limit [Å]3.300
Rmerge0.118
Total number of observations279016

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Number of reflections23854
<I/σ(I)>5.7
Completeness [%]100.0
Redundancy11.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

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7.4

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20

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PROTEIN WAS CRYSTALLIZED FROM 16% PEG 6000, 80MM AMMONIUM SULFATE, 100MM TRIS - HCL, PH 8.5
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein30 (mg/ml)
21dropammonium sulfate40 (mM)
31dropTris-HCl5 (mM)
41dropdithiothreitol1 (mM)
51reservoirPEG600016 (%)
61reservoirammonium sulfate80 (mM)
71reservoirTris-HCl100 (mM)

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