A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis

Trindade, I.B.; Fonseca, B.M.; Matias, P.M.; Louro, R.O.; Moe, E.

doi:10.1107/S2053230X16011419

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
(a) 12% SDS–PAGE gels. Lanes 1 and 2 correspond to the purified SIP fraction before crystallization and dissolved multiple crystals of the SIP, respectively. Lane L corresponds to the protein ladder (labelled in kDa). (b) UV–visible profile of the purified protein. The UV–visible spectrum was measured in a Shimadzu UV-1800 UV–Vis spectrophotometer using a fast scan rate.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 72| Part 9| September 2016| Pages 667-671

doi:10.1107/S2053230X16011419

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