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1ary

;CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS ;

Method: X-RAY DIFFRACTION Dmax: 63.7 Å Quality: GOOD

SAXS Profile

SAXS profile for 1ary

P(r) Distribution

P(r) distribution for 1ary

1. Structure Basics

entry_id1ary
deposition_date1995-04-25
title;CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS ;
keywordsPEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE); PEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE)
methodX-RAY DIFFRACTION

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier20.22
rg_electron19.36
i026566700.00
molecular_weight37150.0 kDa
excluded_volume45167 ų
envelope_volume50373 ų
shell_volume21523 ų
envelope_diameter64.0
shell_rg26.12
envelope_rg19.69
shape_rg19.43
total_rg19.97
total_atoms2546
n_residues336
n_harmonics20
q_range— – 0.5000 −1
n_points101
shell_typedirectional
solvent_density0.3340 e/ų
contrast_shell0.0300 e/ų
crysol_version4.1.3

3. P(r) Analysis (GNOM)

dmax63.7
rg_real20.14
rg_real_error0.32
i0_real2.6570e+07
i0_real_error3.1840e+05
rg_reciprocal20.15
i0_reciprocal26570000.0000
total_estimate0.7584
solution_quality GOOD a GOOD solution
n_peaks2
r_peak_primary25.5
skewness0.255
kurtosis-0.320
angular_range— – 0.3950 −1
current_alpha0.0000
highest_alpha3765000.0000
n_real_points71
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 0.406; Positv: 1.000; Valcen: 0.993; Smooth: 0.989

4. Crystallography & Experiment

5. Entities & Polymer Info (7)

6. Citations (3)

7. Files & Curves (10)