1GA1

CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF IODOTYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)

Summary for 1GA1

• Entry DOI: 10.2210/pdb1ga1/pdb
• Related: 1ga4 1ga6
• Descriptor: SERINE-CARBOXYL PROTEINASE, FRAGMENT OF IODOTYROSTATIN, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: serine-carboxyl proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Pseudomonas sp.; More
• Cellular location: Periplasm: P42790
• Total number of polymer chains: 2
• Total formula weight: 39075.11

Authors

Dauter, Z.,Li, M.,Wlodawer, A. (deposition date: 2000-11-29, release date: 2000-12-13, Last modification date: 2011-07-13)

Primary citation

Dauter, Z.,Li, M.,Wlodawer, A.
Practical experience with the use of halides for phasing macromolecular structures: a powerful tool for structural genomics.
Acta Crystallogr.,Sect.D, 57:239-249, 2001

PubMed Abstract: The crystal structure of pepstatin-insensitive carboxyl proteinase (PCP) from Pseudomonas sp. 101, an enzyme with no overall sequence similarity to any other proteinases of known structure, was solved using crystals soaked in sodium bromide solution and then cryocooled. A data set collected at the bromine peak absorption wavelength was sufficient for calculation of an excellent map and the entire process of phasing and tracing the maps required almost no direct human intervention. The process of structure solution using single-wavelength data was compared with three-wavelength multiwavelength anomalous diffraction (MAD); although the latter resulted in slightly better maps, the use of this much more labor-intensive approach did not significantly improve the ability to solve the structure. The successful phasing approaches are compared with several less successful attempts utilizing other crystal forms of the enzyme and the practical aspects of the use of bromine as a heavy-atom derivative are discussed. In conclusion, the use of halides with single-wavelength diffraction data fulfills the requirements of being a first-choice method of high-throughput structure solution for the emerging field of structural genomics.

PubMed: 11173470
DOI: 10.1107/S0907444900015249

Experimental method

X-RAY DIFFRACTION (1.4 Å)