Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / metalloendopeptidase activity / membrane => GO:0016020 / metal ion binding / plasma membrane Similarity search - Function
Uncharacterised conserved protein UCP006404, peptidase M50/CBS / Peptidase M50 / Peptidase family M50 / Domain in cystathionine beta-synthase and other proteins. / CBS domain / CBS domain / CBS domain profile. / Neutral zinc metallopeptidases, zinc-binding region signature. Similarity search - Domain/homology
Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 2
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Sample preparation
Crystal
Density Matthews: 4.08 Å3/Da / Density % sol: 69.87 %
Crystal grow
Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.8 Details: 0.1 M Tris (pH 8.8), 20% (w/v) PEG400, 50 mM NaCl, 5 mM CaCl2 and 30 mM MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 295K
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Data collection
Diffraction
ID
Mean temperature (K)
Crystal-ID
1
100
1
2
100
1
Diffraction source
Source
Site
Beamline
ID
Wavelength (Å)
SYNCHROTRON
NSLS
X29A
1
1.0809
SYNCHROTRON
NSLS
X29A
2
0.97909, 0.97925
Detector
Type
ID
Detector
Date
ADSC QUANTUM 315
1
CCD
Aug 1, 2007
ADSC QUANTUM 315
2
CCD
Sep 17, 2007
Radiation
ID
Monochromator
Protocol
Monochromatic (M) / Laue (L)
Scattering type
Wavelength-ID
1
Si(111)
SINGLEWAVELENGTH
M
x-ray
1
2
Si(111)
MAD
M
x-ray
2
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
1.0809
1
2
0.97909
1
3
0.97925
1
Reflection
Resolution: 3.3→50 Å / Num. obs: 11853 / % possible obs: 99.3 % / Redundancy: 3.7 % / Biso Wilson estimate: 96.9 Å2 / Rsym value: 0.055 / Net I/σ(I): 14
Reflection shell
Resolution: 3.3→3.42 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 2.4 / Rsym value: 0.485 / % possible all: 99.8
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Processing
Software
Name
Version
Classification
CNS
1.1
refinement
CBASS
datacollection
DENZO
datareduction
SCALEPACK
datascaling
SHELXS
phasing
Refinement
Method to determine structure: MAD / Resolution: 3.3→34.99 Å / Rfactor Rfree error: 0.013 / Data cutoff high absF: 1526734.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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