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231223s1995 xx ||||| 00| ||eng c |
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|a pubmed25n0543.xml
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|a (NLM)16714805
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Fourme, R
|e verfasserin
|4 aut
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|a The Perfection of Protein Crystals Probed by Direct Recording of Bragg Reflection Profiles with a Quasi-Planar X-ray Wave
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|c 1995
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 02.10.2012
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|a Date Revised 22.05.2006
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|a published: Print
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|a Citation Status PubMed-not-MEDLINE
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|a Profiles of Bragg reflections from earth-grown crystals of lysozyme from hen egg-white and collagenase from Hypoderma lineatum were directly recorded with a quasi-planar X-ray wave. One crystal of each protein was chosen for a detailed investigation. Each sample is shown to consist of only a few (three and two, respectively) highly ordered domains, misoriented with respect to each other by a few arc s. The smallest rocking widths were observed for the large domain of the collagenase sample (FWHM corrected for instrumental broadening: 0.0016 degrees for a strong reflection at 3 A resolution). With appropriate improvements, this method might become a quantitative tool for characterizing the perfection of crystals from biological macromolecules
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|a Journal Article
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|a Ducruix, A
|e verfasserin
|4 aut
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|a Ries-Kautt, M
|e verfasserin
|4 aut
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| 700 |
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|a Capelle, B
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of synchrotron radiation
|d 1994
|g 2(1995), Pt 3 vom: 01. Mai, Seite 136-42
|w (DE-627)NLM09824129X
|x 0909-0495
|7 nnns
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| 773 |
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|g volume:2
|g year:1995
|g number:Pt 3
|g day:01
|g month:05
|g pages:136-42
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|a GBV_ILN_2005
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|a AR
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|d 2
|j 1995
|e Pt 3
|b 01
|c 05
|h 136-42
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