A: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 33A B: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 33A C: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 16 HOMOLOG hetero molecules
Mass: 18.015 Da / Num. of mol.: 195 / Source method: isolated from a natural source / Formula: H2O
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Details
Sequence details
ADDITIONAL C-TERMINAL RESIDUES ARE DERIVED FROM THE EXPRESSION VECTOR. ADDITIONAL N-TERMINAL ...ADDITIONAL C-TERMINAL RESIDUES ARE DERIVED FROM THE EXPRESSION VECTOR. ADDITIONAL N-TERMINAL RESIDUES ARE RESIDUAL FROM CLEAVAGE OF GST PURIFICATION TAG
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 3.64 Å3/Da / Density % sol: 66.19 % / Description: NONE
Crystal grow
Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 Details: CRYSTALS WERE GROWN IN SITTING DROPS AT 20C. VPS33A:VPS16 COMPLEX (200 NL; A280 = 7.13, APPROX. 8.7 MG/ML) WAS MIXED 1:1 WITH RESERVOIR SOLUTION AND EQUILIBRATED AGAINST 80 UL RESERVOIRS ...Details: CRYSTALS WERE GROWN IN SITTING DROPS AT 20C. VPS33A:VPS16 COMPLEX (200 NL; A280 = 7.13, APPROX. 8.7 MG/ML) WAS MIXED 1:1 WITH RESERVOIR SOLUTION AND EQUILIBRATED AGAINST 80 UL RESERVOIRS CONTAINING 4% TACSIMATE PH 6.0, 12% PEG 3350 (HAMPTON RESEARCH). CRYSTALS WERE CRYOPROTECTED BY BRIEF IMMERSION IN RESERVOIR SOLUTION SUPPLEMENTED WITH 30% ETHYLENE GLYCOL AND CRYO-COOLED BY PLUNGING INTO LIQUID NITROGEN.
Resolution: 2.6→85.84 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.943 / SU B: 15.437 / SU ML: 0.158 / Cross valid method: THROUGHOUT / ESU R: 0.302 / ESU R Free: 0.22 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.21024
3465
5.1 %
RANDOM
Rwork
0.17594
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obs
0.17762
65003
99.98 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK