Faculty Opinions recommendation of Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Österreichische Akademie der Wissenschaften (APART fellowship 614), the Österreichische Fonds zur Förderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Günter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteins.

2001 ◽  
Author(s):  
Ruma Banerjee
Keyword(s):  
Data Collection ◽  
European Commission ◽  
Alkyl Radical ◽  
Crystallographic Data ◽  
Glutamate Mutase ◽  
Radical Transfer ◽  
Coenzyme B

Advanced Crystallographic Data Collection Protocols for Experimental Phasing

2016 ◽  
pp. 175-191 ◽  
Author(s):  
Aaron D. Finke ◽  
Ezequiel Panepucci ◽  
Clemens Vonrhein ◽  
Meitian Wang ◽  
Gérard Bricogne ◽  
...  
Keyword(s):  
Data Collection ◽  
Crystallographic Data ◽  
Experimental Phasing

The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection

2008 ◽  
Vol 412 (2) ◽  
pp. 257-264 ◽  
Author(s):  
Hans-Petter Hersleth ◽  
Ya-Wen Hsiao ◽  
Ulf Ryde ◽  
Carl Henrik Görbitz ◽  
K. Kristoffer Andersson
Keyword(s):  
Crystal Structure ◽  
Hydrogen Peroxide ◽  
Data Collection ◽  
Intermediate Compound ◽  
Crystallographic Data ◽  
X Rays ◽  
Biologically Relevant ◽  
Short Annealing ◽  
High Valent ◽  
Compound Ii

Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallographic data collection. We have generated and solved the 1.30 Å (1 Å=0.1 nm) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe–O distance of 1.8 Å and O–O bond of 1.3 Å in accordance with a FeII–O–O− (or FeIII–O–O2−) structure. The generation of the peroxy intermediate through reduction of compound III by X-rays shows the importance of using single-crystal microspectrophotometry when doing crystallography on metalloproteins. After having collected crystallographic data on a peroxy-generated myoglobin crystal, we were able (by a short annealing) to break the O–O bond leading to formation of compound II. These results indicate that the cryoradiolytic-generated peroxymyoglobin is biologically relevant through its conversion into compound II upon heating. Additionally, we have observed that the Xe1 site is occupied by a water molecule, which might be the leaving group in the compound II to compound III reaction.

RSPACE – a reciprocal-space modelling tool

1989 ◽  
Vol 22 (6) ◽  
pp. 624-627
Author(s):  
M. R. Harris ◽  
M. Fitzgibbon ◽  
F. Hage
Keyword(s):  
Computer Graphics ◽  
Data Collection ◽  
Reciprocal Space ◽  
Crystallographic Data ◽  
Complex Data ◽  
Educational Tool ◽  
Interactive Computer Graphics ◽  
Area Detector ◽  
The Relationship ◽  
Collection Strategies

RSPACE is an interactive computer-graphics program that models the relationship between crystallographic data-collection hardware and reciprocal space. It is designed to help crystallographers plan efficient complex data-collection strategies for area detector systems, and as an educational tool. Because RSPACE models the interaction of crystal, detector and goniostat geometry in a general way, it is of particular interest to users of area detectors interfaced with multi-axis goniostats.

High-throughput crystallographic data collection at synchrotrons

2007 ◽  
pp. 173-190 ◽  
Author(s):  
Stephen R. Wasserman ◽  
David W. Smith ◽  
Kevin L. D'Amico ◽  
John W. Koss ◽  
Laura L. Morisco ◽  
...  
Keyword(s):  
Data Collection ◽  
High Throughput ◽  
Crystallographic Data

scholarly journals Asymmetry of the Active Site Loop Conformation between Subunits of Glutamate-1-semialdehyde Aminomutase in Solution

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Barbara Campanini ◽  
Stefano Bettati ◽  
Martino Luigi di Salvo ◽  
Andrea Mozzarelli ◽  
Roberto Contestabile
Keyword(s):  
Crystal Structure ◽  
Fluorescence Quenching ◽  
Potassium Iodide ◽  
Active Site ◽  
Catalytic Site ◽  
Crystallographic Data ◽  
Closed Conformation ◽  
Common Precursor ◽  
Coenzyme B ◽  
Loop Conformation

Glutamate-1-semialdehyde aminomutase (GSAM) is a dimeric, pyridoxal 5′-phosphate (PLP)- dependent enzyme catalysing in plants and some bacteria the isomerization of L-glutamate-1-semialdehyde to 5-aminolevulinate, a common precursor of chlorophyll, haem, coenzyme B12, and other tetrapyrrolic compounds. During the catalytic cycle, the coenzyme undergoes conversion from pyridoxamine 5′-phosphate (PMP) to PLP. The entrance of the catalytic site is protected by a loop that is believed to switch from an open to a closed conformation during catalysis. Crystallographic studies indicated that the structure of the mobile loop is related to the form of the cofactor bound to the active site, allowing for asymmetry within the dimer. Since no information on structural and functional asymmetry of the enzyme in solution is available in the literature, we investigated the active site accessibility by determining the cofactor fluorescence quenching of PMP- and PLP-GSAM forms. PLP-GSAM is partially quenched by potassium iodide, suggesting that at least one catalytic site is accessible to the anionic quencher and therefore confirming the asymmetry observed in the crystal structure. Iodide induces release of the cofactor from PMP-GSAM, apparently from only one catalytic site, therefore suggesting an asymmetry also in this form of the enzyme in solution, in contrast with the crystallographic data.

scholarly journals Developing EU environmental standards for the food, drink and milk industries: key environmental issues and data collection

2020 ◽  
Author(s):  
German Giner Santonja ◽  
Panagiotis Karlis
Keyword(s):  
Data Collection ◽  
European Commission ◽  
Environmental Issues ◽  
The European Union ◽  
Policy Integration ◽  
Environmental Standards ◽  
Industrial Emissions ◽  
Best Available Techniques ◽  
Systematic Determination

Abstract Background The European Commission organised the review of the best available techniques reference document for the food, drink and milk industries according to the provisions of the Industrial Emissions Directive (Directive 2010/75/EU). Under this policy, an exchange of information between Member States, industrial organisations, non-governmental organisations promoting the protection of the environment and the European Commission took place. Results A crucial part for developing these EU environmental standards was a systematic determination of the key environmental issues of the food, drink and milk sector. Key environmental issues were defined for emissions to air and water, and for energy and water consumption. The key environmental issues were systematically determined by using four criteria proposed by the European Commission. Moreover, a data collection procedure was designed and real-plant emissions and consumption data were obtained for the first time from a representative variety of food, drink and milk installations across the European Union. Conclusions The development of the EU environmental standards for the food, drink and milk sector are based on a systematic determination of the key environmental issues and on a representative data collection for this sector. This paper also highlights the main normative, organisational and procedural factors addressed during the environmental policy integration carried out to develop these standards.

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