1 idechain identification and crystallographic
R factor.
2 e ligands at 2.2-2.6 A resolution and 17-21%
R factors.
3 ato 3' enhancer is to regulate the levels of
RD factors.
4 antenna-related (danr) genes encode two new
RD factors.
5 s been determined to a resolution of 1.30 A (
R-factor 0.159; R-free 0.213).
6 at the resolution of 1.9 A and refined to an
R-factor 0.191.
7 , a = 29.58 A, b = 54.04 A, c = 40.22 A, and
R-factor =
0.163) revealed that only one acridine of the
8 allography to a resolution of 2.1 A (overall
R-factor =
0.214, free R = 0.248).
9 e) has been determined at 2.37 A resolution (
R-factor =
0.23, R(free) = 0.27).
10 ositively correlated with scores on both PCL-
R factors 1 and 2.
11 been solved and refined at 1.8 A resolution (
R-factor 16.6%; free R-factor 22.8%).
12 ermination of acivicin-modified HpGT (1.7 A;
R(factor) =
17.9%; R(free) = 20.8%) demonstrates that ac
13 crystal structure to a resolution of 2.1 A (
R-factor=
17%).
14 re has been determined to 1.88 A resolution (
R -factor 19.1 %).
15 ructure has been solved to 2.3 A resolution (
R -factor 19.8 %).
16 t effective (quintuple) mutant RC at 2.25 A (
R-factor =
19.6%).
17 ion and the model has been refined to 2.4 A (
R-factor,
19.9%; R-free, 23.9%).
18 ed at 1.8 A resolution (R-factor 16.6%; free
R-factor 22.8%).
19 Glc PPase model was refined to 2.1 A with an
R factor =
22% and R free = 26.6%.
20 and basic helix-loop-helix (bHLH) repressor (
R) factors (
a "P+R" regulatory code), we have identified
21 lues of interproton distances and sixth-root
R factor analysis of experimental intensities indicate t
22 ed at 2.3 A resolution to a crystallographic
R factor and free R factor of 18.2 and 28.2%, respective
23 the potential for acquiring genes from other
R factors and could explain the limited variety of antib
24 data to 3.2 A resolution (1 A=0.1 nm), to an
R-factor and R(free) of 27.3 and 28.6 %, respectively.
25 The final crystallographic
R-factor and R(free) value is 11.0% and 13.2%, respectiv
26 Their relationships to other proposed NMR "
R-factors"
and structure quality assessment scores are a
27 of hydrogen bonds, improved crystallographic
R-factors,
and superior backbone geometry.
28 and the absence of Mg2+ have been refined to
R-factors below 0.2 against data to a nominal resolution
29 The
R-factor between the experimental structure factors and
30 The
R-factor between these predicted swollen capsid structur
31 mined at 2.1-2.2 A resolution and refined to
R-factors between 0.165 and 0.184.
32 Correlation of
R factors,
calculated using the program CORMA with DNA H
33 The complete cross-validation and
R-factor calculation is demonstrated using experimental
34 c regions introgressed from red siskins into
red factor canaries that are required for red coloration
35 icantly upregulated in the skin and liver of
red factor canaries, strongly implicating CYP2J19 as the
36 ta), common canaries (Serinus canaria), and "
red factor"
canaries, which are the hybrid product of cr
37 hains, lower sidechain RMS error and reduced
R factor,
compared to simply placing the best-matching s
38 ctivation but can induce increased levels of
RD factor Dachshund (Dac) and synergize with So and Eya
39 structure and refined to a crystallographic
R-factor equal to 0.183 (R(free) 0.208).
40 2.0 and 1.4 A, respectively, and refined to
R-factors equal 0.163 and 0.145.
41 ression specifically in the eye and that the
RD factors Eyeless and Sine oculis function as direct re
42 The
R-factor for the refined model is 19.7%.
43 ignificant, improvements in dipolar coupling
R-factors for both the working set of couplings used in
44 o larger ensemble sizes do not result in any
R-factor improvement for the cross-validated C alpha-H a
45 R factors indicate the structures fit the experimental N
46 The crystallographic
R factor is 0.177 for 49 242 reflections observed at the
47 X-ray diffraction at 1.45 A resolution; the
R factor is 18.2%.
48 d ag85B crystal structure (1.9 A resolution;
R-factor is 0.195; R(free) is 0.285).
49 The final
R-factor is 0.196 (Rfree = 0.251) for 2sigma data from 7
50 The
R-factor is 17.6% (Rfree of 23.1%) for 4035 reflections
51 The current crystallographic
R-factor is 17.7% for all recorded data (92% complete) t
52 The crystallographic
R-factor is 18.1% for all data from 20 to 2.1 A, and the
53 Quantitatively, the
ring factor is found as an adjustable parameter from the
54 lation in 293- and BHK cell lines expressing
r-factor IX (fIX) and endogenous carboxylase or overexpr
55 ures solved at a resolution of </=2 A and an
R-factor &
lt;/=25%; the latter is based on 131 RNA crystal
56 e was refined at 2.0 A resolution to a final
R -factor of 18.7 %, and Rfreeof 26.7 %.The main feature
57 stereochemistry and a final crystallographic
R factor of 0.162.
58 annealing and restrained least squares to an
R factor of 0.165 for 46,787 reflections.
59 ported at 2.4 A resolution and refined to an
R factor of 0.17.
60 at 1.85 A resolution with a crystallographic
R factor of 0.185.
61 rphous replacement methods and refined to an
R factor of 0.187 at 1.75 A resolution.
62 del has good geometry and a crystallographic
R factor of 0.187 for 11 441 reflections observed betwee
63 at 1.5-A resolution with a crystallographic
R factor of 0.191.
64 le isomorphous replacement and refined to an
R factor of 0.195 (Rfree = 0.272).
65 model has reasonable stereochemistry with an
R factor of 0.195.
66 ethionine-enriched protein and refined to an
R factor of 0.21.
67 ngth anomalous diffraction and refined to an
R factor of 0.231 (Rfree, 0.265).
68 been determined to a resolution of 1.3 A and
R factor of 13.9%.
69 l structure was determined to 1.15 A with an
R factor of 14.9% (Rfree = 17.0%) by multiple-wavelength
70 l structure to 2.5 A resolution with a final
R factor of 15.2% (Rfree = 24.0%).
71 The structure, refined to an
R factor of 15.5% to 1.85 A resolution, is dimeric and h
72 lecules, refines to a final crystallographic
R factor of 16.5%.
73 has been refined to 1.85 A resolution and an
R factor of 16.6% for data collected at -173 degreesC.
74 model and refined at 1.7 A resolution to an
R factor of 16.6%.
75 been determined at 2.3 A resolution with an
R factor of 17.1%.
76 tion to a crystallographic R factor and free
R factor of 18.2 and 28.2%, respectively.
77 n of 2.2 A and refined to a crystallographic
R factor of 18.6%.
78 Se-Met-substituted enzyme to a conventional
R factor of 19.0% (Rfree = 24.2%).
79 ebuilding and refinement the model yields an
R factor of 19.0%, a free R-factor of 28.3%, and good ge
80 ein was completed to 2.3 A and refined to an
R factor of 19.0%.
81 six duplexes in the unit cell, refined to an
R factor of 19.1 for 204 DNA atoms and 43 solvent molecu
82 The structure has been refined to an
R factor of 19.5% at 2.2 A resolution.
83 rmined at 2.2 A resolution and refined to an
R factor of 20.1%.
84 model has been refined to a crystallographic
R factor of 20.3 % and free R-factor of 26.8 % in the re
85 P) kinase p38 has been solved at 2.1-A to an
R factor of 21.0%, making p38 the second low activity MA
86 re of Rad6 refined at 2.6 A resolution to an
R factor of 21.3%.
87 uman NEDD8 refined at 1.6-A resolution to an
R factor of 21.9%.
88 olution of the structure was 2.87 A, with an
R factor of 22%.
89 ength anomalous dispersion and refined to an
R factor of 24.1% to 2.8-A resolution.
90 rix calculations, which yielded a sixth root
R factor of 8.1 x 10(-2).
91 rix calculations, which yielded a sixth root
R factor of 9.1 x 10(-)2 at 250 ms.
92 9 A resolution, respectively, and refined to
R factors of 0.156 and 0.158.
93 A nominal resolutions, with crystallographic
R factors of 0.180 and 0.178, respectively.
94 om a second crystal form and were refined to
R factors of 0.205 and 0.217 (Rfree = 0.255 and 0.263),
95 .5 A resolution, with final crystallographic
R factors of 0.206 (R(free) = 0.255) and 0.190 (R(free)
96 K to 1.8 angstrom resolution and refined to
R factors of 0.211 (113 K) and 0.178 (293 K).
97 etermined to 2.2 A resolution and refined to
R factors of 16.9% and 18.6%.
98 o resolution limits of 1.9A and 2.7A, and to
R factors of 17% and 18%, respectively.
99 their complexes to 2.1-1.9 A resolution with
R factors of 18.7-19.6%.
100 The structures were refined to
R factors of 23% and 24% for the Cd(2+) and Zn(2+) compl
101 ures solved at a resolution of </=3 A and an
R-factor of </=25%, and includes both the large and smal
102 refined by molecular dynamics methods to an
R-factor of 0.095.
103 cture has been refined to a crystallographic
R-factor of 0.151 for data between 10.0- and 1.85-A reso
104 rminus as the search model and refined to an
R-factor of 0.156 (R(free)=0.245) at 1.9 A.
105 19 and refined it at 1.95-A resolution to an
R-factor of 0.157.
106 The structure, refined to an
R-factor of 0.158 at 2.0 A resolution, reveals XAN bound
107 refined using data from 10 A to 2.1 A to an
R-factor of 0.16.
108 ginine model has a standard crystallographic
R-factor of 0.162, with good geometry at 2.5 A resolutio
109 uding 552 molecules of solvent, and gives an
R-factor of 0.163.
110 anomalous diffraction data and refined to an
R-factor of 0.164 (R(free)=0.199) at 2.3 A resolution.
111 bic methyl-alpha-Man complex refined with an
R-factor of 0.167 (all data) includes 12 bound sugar lig
112 The crystal structure was refined to an
R-factor of 0.17 at 0.21-nm resolution.
113 l of the chymostatin arginine complex has an
R-factor of 0.174, with good geometry using data to 2.1
114 cement and refined at 2.4 A resolution to an
R-factor of 0.18 (Rfree = 0.24).
115 method, and the model has been refined to an
R-factor of 0.18 for all data in the range 8.0-1.98 A re
116 on analysis to a resolution of 1.6 A with an
R-factor of 0.18.
117 d at 2.3 A and refined to a crystallographic
R-factor of 0.18.
118 rystal structure of Y447H (2.1 A resolution,
R-factor of 0.181) is essentially unchanged from that of
119 ues and refined by simulated annealing to an
R-factor of 0.183 at 2.93 A resolution.
120 olvent flattening and has been refined to an
R-factor of 0.185, with rms deviations from ideal bond d
121 at 2.05 A resolution with a crystallographic
R-factor of 0.186 and R-free of 0.231.
122 has been determined and refined to a working
R-factor of 0.186 at 1.9 A resolution.
123 (AAPF) has been determined and refined to an
R-factor of 0.189 at 2.4 A resolution.
124 1)2(1)2(1)) has been solved to 2.5 A with an
R-factor of 0.193.
125 B model is refined against 1.8 A data, to an
R-factor of 0.196 (R(free) is 0.276), and includes all r
126 at 1.9 A to a conventional crystallographic
R-factor of 0.198 and Rfree of 0.239.
127 method, and the model has been refined to an
R-factor of 0.20 for all nonzero data from 8 to 1.8 A.
128 .3-A resolution and a final crystallographic
R-factor of 0.204.
129 D consists of residues 172 to 404 and has an
R-factor of 0.205 (Rfree=0.249) for 9696 reflections bet
130 the MAD phasing technique, and refined to an
R-factor of 0.209.
131 ed, and the structure has been refined to an
R-factor of 0.214, using the 1421 reflections with F > 2
132 by molecular replacement and refined with an
R-factor of 0.215 (R(free) = 0.266).
133 .2 A resolution by simulated annealing to an
R-factor of 0.218.
134 has been determined and refined to the final
R-factor of 0.219 at the resolution of 2.1 A.
135 he asymmetric unit and has been refined to a
R-factor of 0.222 (R-free = 0.257) for 29,702 reflection
136 The final refined PfALDO model has an
R-factor of 0.239 and an R-free of 0.329 with respect to
137 inal R(free) of 15.0% and a crystallographic
R-factor of 11.6%.
138 X-ray diffraction data to a crystallographic
R-factor of 12.92%.
139 e crystal structures have been refined to an
R-factor of 14.2% at resolutions of 2.0 and 1.9 A.
140 solved and refined at 2.3 A resolution to an
R-factor of 14.3%.
141 cement at 1.6 A resolution and refined to an
R-factor of 15.0% (free R = 18.6%).
142 isiae at 1.1 angstrom and a crystallographic
R-factor of 15.3%, revealing seven authentic repeats.
143 l resolution of 2.1 A and a crystallographic
R-factor of 15.4% for all measured X-ray data.
144 (beta Glu6-->Val) at 2.05 A resolution to an
R-factor of 16.5% (free R=21.5%) using crystals isomorph
145 ved to resolution limits of 1.68 A and to an
R-factor of 17% using the recombinant protein expressed
146 s been determined to 1.8 A and refined to an
R-factor of 17% while the structure from the orthorhombi
147 n and has been refined to a crystallographic
R-factor of 17.0%.
148 tion data to a conventional crystallographic
R-factor of 17.0%.
149 e was refined at a resolution of 2.1 A to an
R-factor of 17.3%, that of the S. typhimurium enzyme at
150 ion analysis to a resolution of 2.3 A and an
R-factor of 17.7%.
151 xed with CK17, refined to a crystallographic
R-factor of 17.8% at 2.5 angstrom resolution.
152 at 2.4 A to a conventional crystallographic
R-factor of 17.9 % (R(free) 21.1 %).
153 e been determined to 2.2 A resolution and an
R-factor of 17.9 and 20.8%, respectively.
154 ominal resolution of 1.8 A and refined to an
R-factor of 17.9%.
155 (pTyr), and the structure was refined to an
R-factor of 18.1% at 1.85 A.
156 microM), and the structure was refined to an
R-factor of 18.2% at 1.9 A resolution.
157 ominal resolution of 1.8 A and refined to an
R-factor of 18.2% for all measurement X-ray data.
158 uciferase has been refined to a conventional
R-factor of 18.2% for all recorded synchrotron data betw
159 ture was refined to a final crystallographic
R-factor of 18.2% with good stereochemical parameters.
160 TG)(2) has been determined and refined to an
R-factor of 18.3% using X-ray data up to 1.2 A resolutio
161 d derivative d(CG5BrCGAG), and refined to an
R-factor of 18.6% for 120 nonhydrogen nucleic acid atoms
162 ed at 2.5 A resolution to a crystallographic
R-factor of 18.7%.
163 The model was refined to a crystallographic
R-factor of 18.9% and a free R-factor of 28.4% using all
164 omorphous replacement and refined to a final
R-factor of 19.0%.
165 to 1.55 A resolution and a crystallographic
R-factor of 19.0%.
166 model has been refined to a crystallographic
R-factor of 19.1% for all measured X-ray data from 30 to
167 raction phasing techniques and refined to an
R-factor of 19.3% at 2.4 A resolution.
168 nitrificans was determined and refined to an
R-factor of 19.3% at 2.6 A resolution.
169 resolution and refined to a crystallographic
R-factor of 19.4%.
170 model, and refined at 2.7 A resolution to a
R-factor of 19.5 %.
171 The refined structure has an
R-factor of 19.6% (data between 65 and 1.86 A resolution
172 ring and refined to a final crystallographic
R-factor of 19.6% using data from 25.0 A to 1.65 A.
173 tor switch, FliM, to 1.5A resolution with an
R-factor of 19.6%.
174 .6 angstrom resolution to a crystallographic
R-factor of 19.7% and a free R-factor of 26.1%.
175 typhimurium enzyme at 1.7 A resolution to an
R-factor of 19.8%.
176 A resolution, and the final structure has an
R-factor of 19.8%.
177 he final model of CSK has been refined to an
R-factor of 19.9 % (Rfree=28.7 %) at 2.4 A resolution.
178 ar replacement method and refined to a final
R-factor of 19.9% (Rfree 22.2%).
179 model was refined at 3.0 A resolution to an
R-factor of 19.9% using 21 899 reflections, with Rfree 2
180 has been solved to 2.3 A resolution with an
R-factor of 20.3% and a free R-factor of 22.3%.
181 S) and was refined at 2.0 A resolution to an
R-factor of 20.6% (R-free=25.2%).
182 lar replacement method and was refined to an
R-factor of 20.7% with an Rfree of 28.8%.
183 ermined to 2.65 A and has been refined to an
R-factor of 21%.
184 arch model and refined to a crystallographic
R-factor of 21.2% and an R-free value of 28.8%.
185 odel is refined at 1.95 A resolution with an
R-factor of 21.3% and R-free 28.3%.
186 2.6 A resolution data to a crystallographic
R-factor of 21.4% (Rfree is 29.7%).
187 d to 1.5 A resolution and refined to a final
R-factor of 21.6% (R-free 25.1%).
188 ximum resolution of 2.40 A and refined to an
R-factor of 22% (R(free)=26%).
189 s three molecules in the asymmetric unit, an
R-factor of 22.0%, and an R(free) of 27.2% (for 10% of t
190 olution with an R-factor of 20.3% and a free
R-factor of 22.3%.
191 asein kinase-1 refined to a crystallographic
R-factor of 22.4% at 2.8 A resolution.
192 raphic symmetry (NCS) constraints and has an
R-factor of 22.7% and an R-free of 25.5%.
193 mulated annealing Cartesian refinement to an
R-factor of 23.2 and free R-factor of 29.7.
194 resolution and refined to a crystallographic
R-factor of 23.4% with good geometry.
195 been refined at a resolution of 2.1 A to an
R-factor of 23.5% and an R(free) of 27.4%.
196 refined the structure to a crystallographic
R-factor of 24.0%.
197 ned at 2.1 A resolution with an Rfree and an
R-factor of 25.1 and 20.4%, respectively, displays highl
198 rystallographic R-factor of 19.7% and a free
R-factor of 26.1%.
199 crystallographic R factor of 20.3 % and free
R-factor of 26.8 % in the resolution range of 10-2.05 A.
200 he experimental diffraction amplitudes to an
R-factor of 28% at 3.5 angstrom resolution with strict g
201 he model yields an R factor of 19.0%, a free
R-factor of 28.3%, and good geometry with root-mean-squa
202 rystallographic R-factor of 18.9% and a free
R-factor of 28.4% using all data between 25 and 2.3 A an
203 n refinement to an R-factor of 23.2 and free
R-factor of 29.7.
204 and the refined structure was derived to an
R-factor of 36.7% (R(free) 37.9%) by standard crystallog
205 egenerate) modes produce a structure with an
R-factor of 45%, which is further reduced to 43.9% after
206 es as adjustable parameters yielded a lowest
R-factor of 6.3%.
207 oduced a three-dimensional model with an NMR
R-factor of 7%.
208 nt parameters, was refined to a conventional
R-factor of 7.5% and Rfree of 8.7%, making it the most p
209 ta was such as to allow for refinement to an
R-factor of 9.1% and an R(free) of 11.2%.
210 )] are reported at 2.0-2.2 A resolution with
R-factors of 0.0.159-0.179.
211 roacarbose and acarbose have been refined to
R-factors of 0.147 and 0.131 against data to 1.7- and 2.
212 termined to resolutions of 1.7 and 1.8 A and
R-factors of 0.171 and 0.176, respectively.
213 acidin at 298 and 100 K have been refined to
R-factors of 0.171 and 0.206 against data to 2.8 and 2.5
214 acidin at 298 and 100 K have been refined to
R-factors of 0.188 and 0.206 against data to 2.8 A and 2
215 plexes have been refined to crystallographic
R-factors of 0.189 and 0.178, respectively, at 2.7 A res
216 re refined to 2.2- and 2.5-A resolution with
R-factors of 0.190 and 0.217, respectively.
217 The final structures had
R-factors of 0.199 at 1.85-A resolution and 0.155 at 1.6
218 ns ranging from 2.6 to 2.0 A, and refined to
R-factors of 14.5-19.5%.
219 have been refined at 1.75 A to final working
R-factors of 15.4% and 16.4%, respectively.
220 rystal forms to 2.1 and 2.3 A resolution and
R-factors of 17% and 19%, respectively.
221 and refined to 2.12 A with working and free
R-factors of 19.7 and 22.9 %, respectively.
222 resolutions of 2.5A and 2.3A, and refined to
R-factors of 19.7% and 21.5%, respectively.
223 e refined with good stereochemistry to final
R-factors of 21.1 and 21.9%, respectively.
224 d at 1.9 A resolution and refined to a final
R: factor of 19.9% and R(free) of 23.3% for 2862 reflect
225 o complexes were refined to crystallographic
R-factors (
R(free)) of 0.141 (0.186) and 0.138 (0.202),
226 l resistance (ars) operon of the conjugative
R-factor R773 confers resistance to arsenical and antimo
227 demonstrate a direct mechanism by which the
RD factors regulate ato expression and suggest an import
228 The high
R factor results from structural disorder and many weak
229 binding site for the retinal determination (
RD) factor Sine oculis (So).
230 Furthermore the
RD factors So and Eyes absent (Eya) are required for 2.8
231 elded improved model geometry and lower free
R factors than alternate refinement methods.
232 ined to a resolution of 2.0 A or better with
R-factors that range from 16.1% to 17.5%.
233 e protein model reduced the crystallographic
R factor to 18.8% for all measured X-ray data from 30 to
234 24-fold NCS constraints further reduced the
R-factor to 20.4% and the R-free to 23.2%.
235 An
R factor used for characterizing the quality of the reco
236 A decrease of the crystallographic
R-factor value from approximately 72% to approximately 4
237 clavulanate at a resolution of 1.7 A with an
R-factor value of 0.180 and R-free value of 0.212 for th
238 yl tetrahydropteroylglutamate, refined to an
R-factor value of 17.4 % and R(free) value of 19.6 %.
239 The crystallographic
R-factor was 19.4% (33 497 reflections) for 7031 protein
240 Strains with F or F-like
R factors were consistently more sensitive to bile salts