Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma

A. L. Carvalho; J. M. Dias; L. Sanz; A. Romero; J. J. Calvete; M. J. Romão

doi:10.1107/S0907444901009805

Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma

A. L. Carvalho, J. M. Dias, L. Sanz, A. Romero, J. J. Calvete, M. J. Romão

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

The purification, crystallization and identification by X-ray diffraction analysis of a horse kallikrein is reported. The protein was purified from horse seminal plasma. Crystals belong to space group C2 and the structure was solved by the MIRAS method, with two heavy-atom derivatives of mercury and platinum. X-ray diffraction data to 1.42 Å resolution were collected at the ESRF synchrotron-radiation source.

Original language	English
Pages (from-to)	1180-1183
Number of pages	4
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	8
DOIs	https://doi.org/10.1107/S0907444901009805
Publication status	Published - 23 Aug 2001

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abstract = "The purification, crystallization and identification by X-ray diffraction analysis of a horse kallikrein is reported. The protein was purified from horse seminal plasma. Crystals belong to space group C2 and the structure was solved by the MIRAS method, with two heavy-atom derivatives of mercury and platinum. X-ray diffraction data to 1.42 {\AA} resolution were collected at the ESRF synchrotron-radiation source.",

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AU - Dias, J. M.

AU - Sanz, L.

AU - Romero, A.

AU - Calvete, J. J.

AU - Romão, M. J.

PY - 2001/8/23

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AB - The purification, crystallization and identification by X-ray diffraction analysis of a horse kallikrein is reported. The protein was purified from horse seminal plasma. Crystals belong to space group C2 and the structure was solved by the MIRAS method, with two heavy-atom derivatives of mercury and platinum. X-ray diffraction data to 1.42 Å resolution were collected at the ESRF synchrotron-radiation source.

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Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma

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