Electronic Resource
Copenhagen
:
International Union of Crystallography (IUCr)
Applied crystallography online
14 (1981), S. 439-443
ISSN:
1600-5767
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Geosciences
,
Physics
Notes:
Polar coordinates of a Kendrew model of α-chymotrypsin (α-CHT) have been measured with a surveyor's transit and a cathetometer to a high degree of accuracy and precision. Bond distances calculated independently for more than 200 independent amino-acid residues have standard deviations of 0.10 Å or less, the torsion angle ω has a standard error of 7°, and the τ angle is precise to 3°. The measured coordinates of about 1800 non-hydrogen atoms of one molecule of the α-CHT dimer fit a set of idealized polypeptide coordinates with a r.m.s. deviation of 0.17 Å, while the average deviation is 0.15 Å.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0021889881009722
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