Published September 28, 2016 | Version v1
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MAD diffraction images for yeast 5-aminolevulinic acid dehydratase (ALAD).

  • 1. UCL

Description

Selenomethionine multiwavelength anomalous dispersion (MAD) diffraction images for the original structure determination of 5-aminolevulinic acid dehydratase (ALAD) from yeast collected at the bending magnet beamline BM14, ESRF, Grenoble (25-27 Sept 1996). There are separate folders for the data from different wavelengths (l1 is the edge dataset, l4 is the edge inverse beam, l2 is the peak, l5 and l55 are the peak inverse beam (l55 is an overlapping continuation of l5 due to beam loss), l3 is the remote and l6 is the remote inverse beam). The seoa folder contains the selenium 'optimised anomalous' peak data. The images were collected with a Mar Research image plate and each folder has a file called 'mos.com' giving the data collection parameters for that run except for the exposure times which were 45 seconds per image for both l1 and l2, 55 seconds per image for the remote l3 and 120 seconds per image for the optimised anomalous collection (seoa). The latter dataset does not have a file listing the parameters which were: crystal-to-detector distance 275mm, delta-phi 1 degree, wavelength 0.9791 Angstroms, big-MAR format (note other datasets were collected in small-MAR format). 

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References

  • P.T.Erskine, N.Senior, S.Awan, R.Lambert, G.Lewis, I.J.Tickle, M.Sarwar, P.Spencer, P.Thomas, M.J.Warren, P.M.Shoolingin-Jordan, S.P.Wood, and J.B.Cooper. ‘X-ray structure analysis of 5-aminolaevulinate dehydratase, a hybrid aldolase’. Nature Structural Biology (1997) 4, 1025-1031.