Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7A43

Fluoroacetate Dehalogenase measured by serial femtosecond crystallography

Summary for 7A43
Entry DOI10.2210/pdb7a43/pdb
DescriptorFluoroacetate dehalogenase, CHLORIDE ION (3 entities in total)
Functional Keywordsdehalogenase, serial femtosecond crystallography, hydrolase
Biological sourceRhodopseudomonas palustris
Total number of polymer chains2
Total formula weight68218.23
Authors
Mehrabi, P.,Schulz, E.C.,Buecker, R. (deposition date: 2020-08-19, release date: 2021-04-07, Last modification date: 2024-01-31)
Primary citationMehrabi, P.,Bucker, R.,Bourenkov, G.,Ginn, H.M.,von Stetten, D.,Muller-Werkmeister, H.M.,Kuo, A.,Morizumi, T.,Eger, B.T.,Ou, W.L.,Oghbaey, S.,Sarracini, A.,Besaw, J.E.,Pare-Labrosse, O.,Meier, S.,Schikora, H.,Tellkamp, F.,Marx, A.,Sherrell, D.A.,Axford, D.,Owen, R.L.,Ernst, O.P.,Pai, E.F.,Schulz, E.C.,Miller, R.J.D.
Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison.
Sci Adv, 7:-, 2021
Cited by
PubMed Abstract: For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution.
PubMed: 33731353
DOI: 10.1126/sciadv.abf1380
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

227344

数据于2024-11-13公开中

PDB statisticsPDBj update infoContact PDBjnumon